Crystallography related career opportunities, post docs and related positions in the crystallography community. If you wish to place your job opportunity on the Hampton Research website, submit the details to tech@hrmail.com.
The Frederick National Laboratory for Cancer Research is hiring a Research Associate II (Structural Biology). The RA-II will work in the NCI RAS Initiative program to support our mission in understanding RAS biology and developing lead compounds against RAS-driven cancers. Basic qualification is a Bachelor's degree with 5 years of experience in biomedical research.
The Center for Therapeutics Discovery (C3TD) was recently established with the mission to promote the translation of basic science discoveries by Cleveland Clinic researchers into new therapeutics. We have established a pipeline of innovative research programs directed toward improving patient care with a true bench-to-bedside vision. To achieve these goals, we use state of the art technologies in small molecule library screening, fragment-based methods, X-ray crystallography, computational tools, and target validation towards generating starting points for nascent hit-to-lead and lead optimization campaigns.
Postdoctoral structural biologists will have the opportunity to aid in the discovery and development of small molecule inhibitors across multiple disease areas, including oncology, inflammation, cardiovascular and neuroscience. Structural biology fellows will play a vital role in the drug discovery process by solving novel protein structures and protein-ligand complexes, thereby enabling structure-based drug design. Additionally, fellows will help with the development of biochemical assays for the purpose of small molecule drug screening, target validation, and SAR campaigns. This position offers the ability to work on a variety of therapeutically relevant proteins, protein-protein complexes and extensive opportunities to collaborate with CC researchers.
Cleveland Clinic’s Lerner Research Institute is the biomedical research institute of the Cleveland Clinic and represents 1,400 researchers and support personnel in 180 laboratories across 12 departments. The Lerner is one of the largest research institutes in the nation, consistently ranking in the top 10 in National Institutes of Health funding, a benchmark of research success.
The New York Structural Biology Center (NYSBC) is a shared research organization, owned and operated by nine eminent research universities and medical schools in the New York area. NYSBC is devoted to advancing structural and functional characterization of biological processes through technology development for cutting-edge biomedical research. X-ray crystallography is a crucial component of NYSBC activity, and the NYX Microdiffraction Beamline has been developed by NYSBC at the National Synchrotron Light Source II (NSLS-II) to support this work.
NYSBC seeks a Scientist to join the NYX beamline team for NSLS-II sector 19-ID at Brookhaven National Laboratory (BNL) to help steer further development of macromolecular crystallography at NYX. The new scientist will be employed by NYSBC organization and stationed at its NYX beamline at NSLS-II. The successful candidate will establish relevant research projects in collaboration with NYSBC scientists, groups at its constituent institutions, or with BNL structural biologists and other groups. These projects will exploit the unique qualities of the NYX beamline and can be coordinated with the NSLS-II life science programs.
Responsibilities will include interacting and assisting the scientific user community and visiting scientists with their data collections and structure solving. In addition, the new scientist will advance the beamline’s technical capabilities by initiating or conceiving upgrades of its hardware and software for the benefit of the structural biology community at NYSBC and beyond.
Salary level will be commensurate with qualifications and experience.
•	Demonstrated success in leading scientific or technical groups or projects.
Tenure-track beamline scientist position in macromolecular crystallography group at the Photon Science Division, Paul Scherrer Institut (https://www.psi.ch/macromolecular-crystallography/). This position offers a unique opportunity to develop and operate a dedicated serial femtosecond crystallography (SFX) station at the SwissFEL. Detailed information and the online application portal can be found at https://www.psi.ch/pa/stellenangebote/2000.
Enquiries about the application process can be sent to the HR team at personnel@bioc.cam.ac.uk. Please quote reference PH18815 on your application and in any correspondence about this vacancy.
A postdoctoral position is available for a highly motivated biochemist/structural biologist interested in studying molecular mechanisms of cell signaling by ubiquitin and ubiquitin-like proteins. Available projects in the laboratory provide excellent training opportunities as they involve a multidisciplinary approach that combines X-ray crystallography, cryo-electron microscopy, biochemical/biophysical techniques, and cell-based assays.
Candidates should hold a recently obtained PhD in structural biology, biochemistry, or a related area and should be skilled in standard molecular biology techniques and recombinant protein expression and purification. Candidates with demonstrated expertise in X-ray crystallography and/or single particle cryo-electron microscopy are preferred.
Interested candidates should e-mail a cover letter, CV, and the names of three references to olsensk@musc.edu. The position will remain open until filled.
One junior research fellow to study the biochemical and structural features of a G-protein coupled receptor involved in the remyelination of the central nervous system, within the framework of a multicentric project funded by a two-year grant from the Italian Multiple Sclerosis Foundation (FISM).
One post-doctoral research fellow to study the biochemistry and structural basis of self-recognition by B-cell receptors derived from chronic lymphocytic leukaemia patients. The project involves the structural determination to high resolution of the BCRs, the characterization of their mutual binding, and the development of antagonists based on the 3D structures (Minici et al., Nat Commun 2017). The position is funded by a three-year grant from Worldwide Cancer Research.
The successful candidates will join a dynamic group of structural biologists within one of the top-rated biomedical research institutions in Europe to perform structural and functional studies using a combination of biophysical techniques (SPR, ITC, AUC), mutagenesis, cell-based assays, X-ray crystallography and cryo-EM. We are searching for someone with a strong interest in the structure-function relationship of biological macromolecules that is creative, hard-working and willing to tackle challenging, high-rewarding projects.
Salary will be commensurate to experience. Your application should be sent to degano.massimo@hsr.it including your curriculum vitae, a 1-page personal statement on previous experience and your research interests, name and email address of former supervisor(s) that can provide reference.
Applications are invited for a post-doctoral position in the group of Bostjan Kobe at the School of Chemistry and Molecular Biosciences (SCMB), University of Queensland, Brisbane, Australia.
We are searching for a motivated candidate, ideally with experience with cryo-electron microscopy, and/or other structural biology and protein biochemistry techniques, to study the structural basis of function of proteins involved in innate immunity pathways in plants. For some of our recent publications on related topics, please see https://www.ncbi.nlm.nih.gov/pubmed/28159890 , https://www.ncbi.nlm.nih.gov/pubmed/28759049 and https://www.ncbi.nlm.nih.gov/pubmed/24744375 .
University of Queensland is one of Australia's top universities. SCMB combines the disciplines of chemistry, biochemistry & molecular biology, microbiology and parasitology into a single academic unit. SCMB is situated in the beautiful St. Lucia campus on the Brisbane River.
New state-of-the art facilities for cryo-EM are currently being installed and will be available on-campus later in the year (including CRYO ARM 300 and CRYO ARM 200 JEOL field-emission cryo-electron microscopes with direct electron detectors for single-particle analysis). Facilities for high-throughput crystallization (Mosquito robots, Rock Imagers) and various biophysical techniques (MALS, ITC, SPR etc) are also available on-campus, and there is regular access to the Australian Synchrotron.
Brisbane is one of Australia's most liveable cities and has a fantastic subtropical climate. It is only a short drive from Australia's best beaches and provides opportunities for all sorts of outdoors and cultural activities.
The salary will be according to qualifications and experience. The positions are for 2 years, with possible extension subject to funds. The starting date is flexible. The application deadline is 10 May 2019. Please see the links below for details of the positions and application procedures.
Please contact Bostjan Kobe (telephone: +617-3365-2132, email b.kobe@uq.edu.au) for further information.
A post-doctoral position is available to study the role of transcription factors in hematopoiesis and leukemogenesis at the structural level in the laboratory of Susan Chan and Philippe Kastner, at the Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC) in Strasbourg, France (http://www.igbmc.fr/research/department/2/team/18/).
Applicants are expected to have a strong and demonstrable track record in protein biochemistry and X-ray crystallography; experience with cryoEM is a plus but not a requirement.
We welcome highly qualified and motivated individuals, with a recently obtained PhD in structural biology and first author publications in peer-reviewed international journals, who can work easily in a multi-lab consortium. This position is available immediately and is funded for two years.
The IGBMC is a leading European research institute that aims to understand human disease and basic biological mechanisms at the molecular and atomic levels, with state-of-the-art facilities and a vibrant, international scientific community. The working language is English.
Please send a detailed CV with list of publications, a letter of motivation, and the names of three references to Susan Chan and Philippe Kastner (scpk@igbmc.fr).
The Lee lab in the Department of Pharmacology at the Yale School of Medicine has an immediate opening for a highly motivated Postdoctoral Associate to investigate the molecular mechanism of endocrine Fibroblast Growth Factor (FGF) signaling. Endocrine FGFs, which include, FGF15/19, FGF21, and FGF23, activate signaling via FGF receptors and require binding to the Klotho family of surface receptors; FGF23 signaling requires a-Klotho, while FGF15/19 and FGF21 signaling requires ß-Klotho. The research in our laboratory is focused on the structural elucidation, biophysical and biochemical analyses of complexes involved in endocrine FGF signaling.
Applicants should have a PhD in biochemistry, biophysics or a related field and should have extensive experience in recombinant protein production, as well as excellent written and oral communication skills. Experience in structural biology techniques (X-ray crystallography or cryo-EM), mammalian cell culture and quantitative biophysical analyses are also desirable, but not necessary.
Interested candidates should send a current CV, a statement of research interests, and the names and contact information of two references to Sangwon Lee (s.lee@yale.edu).
The Mousa Laboratory at the University of Georgia (UGA) Center for Vaccines and Immunology (CVI) https://vet.uga.edu/cvi in Athens, GA is seeking a creative and enthusiastic postdoctoral fellow to drive forward a research project focused on antibody-antigen interactions. This is a multidisciplinary project with enormous training opportunity in human immunology, virology, and structural biology, including X-ray crystallography and electron microscopy. The Mousa Laboratory studies monoclonal antibodies from humans, mice, and nonhuman primates as therapeutics and to inform vaccine design. The project will focus on the isolation of antibodies, and the immunological and structural characterization of antibody interactions with Pneumovirus and Paramyxoviruses. The postdoctoral fellow also has the opportunity to design protein vaccine constructs informed by structural data and to examine the experimental vaccines in mice and nonhuman primates directly or collaboratively.
The Mousa Laboratory uses a number of techniques that offer high potential for training including: X-ray crystallography, electron microscopy, flow cytometry analysis and sorting, protein biochemistry, biolayer interferometry, virus growth and neutralization analysis, enzyme-linked immunosorbent assays, and monoclonal antibody isolation from human, mouse, and nonhuman primate B cells, among many other techniques. The postdoctoral fellow will be expected to design and conduct research within a specified field while receiving advanced training from a designated Principal Investigator to enhance professional skills and research independence needed for pursuit of a career. The postdoctoral fellow will be expected to design and evaluate experiments, develop new ideas and promote current research, and prepare and publish scientific manuscripts under the direction of the Principal Investigator. The postdoctoral fellow may be responsible for operation of scientific equipment. The postdoctoral fellow may be responsible for teaching techniques to others, including training of students and supervision of research staff.
Positions are temporary appointments as a research trainee. Funding for this position is available for at least two years. The initial appointment is for one year, and renewal is expected if progress is satisfactory and funds are available. Appointments cannot exceed five years.
MINIMUM QUALIFICATIONS: A doctoral degree or equivalent (Ph.D., M.D., ScD., D.V.M., etc.) in an appropriate field is required. Excellent scientific writing ability and strong oral communication skills are required, as is the ability to work effectively and collegially with colleagues.
ADDITIONAL PREFERRED QUALIFICATIONS: Previous experience working with protein expression and crystallization of viral proteins is preferred, but not required. Previous experience with X-ray crystallography and/or electron microscopy is preferred.
SCIENTIFIC ENVIRONMENT: The CVI at UGA is a unique and collaborative research environment currently housing four research laboratories focusing primarily on respiratory pathogens and emerging infectious diseases. The Mousa Lab is housed in the CVI and trainees have generous bench space, and access to state of the art instrumentation including an OctetRED384 system. UGA houses a Mosquito drop-setting robot, a state of the art in-house X-ray beamline, and negative-stain electron microscopes. UGA is a member of the Southeast Regional Access Collaborative Access Team (SER-CAT) at Argonne National Laboratory, and abundant beamtime is available. We also have access to the Electron Microscopy facility at Emory University, which includes a FEI Talos Arctica 200 KV cryo-electron microscope.
The University of Georgia (UGA), a land-grant and sea-grant university with statewide commitments and responsibilities is the state's oldest, most comprehensive, and most diversified institution of higher education (http://www.uga.edu/). UGA is currently ranked among the top 20 public universities in U.S. News & World Report. The University's main campus is located in Athens, approximately 65 miles northeast of Atlanta. UGA employs approximately 1,800 full-time instructional faculty and more than 7,600 full-time staff. The University's enrollment exceeds 36,000 students including over 27,500 undergraduates and over 8,500 graduate and professional students.
Interested applicants should send their CV and list of 2-3 references to Jarrod Mousa, Ph.D. at jarrod.mousa@uga.edu.
Wen, X., Mousa, J.J., Bates, J. Lamb, R.A., Crowe, J.E., Jardetzky, T.S. Structural basis for antibody cross-neutralization of respiratory syncytial virus and human metapneumovirus. Nature Microbiology 2, 2017, 16272.
Mousa, J.J., Kose, N., Matta, P., Gilchuk, P., Crowe, J.E. A novel pre-fusion conformation-specific neutralizing epitope on the respiratory syncytial virus fusion protein. Nature Microbiology 2, 2017, 16271.
Mousa, J.J., Sauer, M.F., Sevy, A.M., Finn, J.A., Bates, J.T., Alvarado, G., King, H.G., Loerinc, L.B., Fong, R.H., Doranz, B.J., Correia, B., Kalyuzhniy, O., Wen, X., Jardetzky, T.S., Schief, W.R., Ohi, M.D., Meiler, J., Crowe, J.E. Structural basis for non-neutralizing antibody competition at antigenic site II of the respiratory syncytial virus fusion protein. Proceedings of the National Academy of Sciences USA 2016, 113, E6849-E6858.
Title: Postdoctoral position available in the Conn Lab, Dept. of Biochemistry, Emory University School of Medicine.
An NIH-funded postdoctoral position is available immediately in the Conn lab in the Department of Biochemistry, Emory University School of Medicine, in Atlanta, GA. This position will be part of our on-going studies of the molecular regulation of human innate immune proteins by viral and cellular non-coding RNAs, in collaboration with Dr. Anice Lowen’s group (Microbiology and Immunology, Emory University School of Medicine).
The ideal candidate will have a recent PhD with experience in macromolecular X-ray crystallography; additional skills in molecular biology, protein expression/ purification, other biochemical or biophysical approaches (e.g. mass spectrometry, HDX-MS) and/ or working with RNA would also be an advantage. Candidates with demonstrated success these or related areas and a strong commitment to learning X-ray crystallography will also be considered.
To apply, please e-mail a CV including a list of publications, a brief statement of experience and scientific interests, and contact information for 2-3 references to gconn@emory.edu.
A postdoctoral position in structural biology is available as of June 1st, 2019 in the laboratory of Dr. Aishwarya Prakash at the Mitchell Cancer Institute (MCI) part of the University of South Alabama in Mobile, AL, USA.
We are seeking a highly motivated individual to join a motivated, productive, and hardworking research team. The candidate will carry forth two or three research projects and be a part of a close-knit, collaborative environment at the Mitchell Cancer Institute.
The laboratory is interested in studying complexes involved in the repair of mitochondrial DNA via the base excision repair pathway (BER). More specifically, the lab is involved in studying the role of DNA glycosylases in the repair of the mitochondrial genome. The laboratory uses a combination of cellular, biochemical, and biophysical approaches to study the complexes formed during BER. Some of these techniques include in vitro binding, activity, and repair assays, multi-angle light scattering, X-ray crystallography, and SAXS. The laboratory is equipped with a state-of the art X-ray diffraction unit and other shared resources available at MCI. More recently the laboratory has been involved with studying the role of DNA glycosylases in cells using CRISPR gene editing and microscopy approaches.
Applications will be reviewed until the position is filled. Interested applicants should send a curriculum vitae, and three letters of reference to mciapjobs@gmail.com.
We (Murali Laboratory at Cedars-Sinai Medical Center, Los Angeles) are seeking an experienced Structure Biologist/X-ray crystallographer. The position is at the Senior Scientist (Project Scientist) level and will be filled as soon as possible.
5) At least 2-3 years of post-doctoral experience in protein crystallization and structure determination and experience in synchrotron-based structure biology experiments.
7) Experience in Thermal shift assay, ELISAs, protein-DNA complex preparation and some experience in drug development including Fragment based approaches are highly desirable.
We are seeking a highly motivated postdoctoral fellow to join the Syun-Ru Yeh Laboratory in the Department of Physiology and Biophysics at the Albert Einstein College of Medicine. The postdoctoral fellow will take a lead in (1) elucidating structure and function relationships of two immunotherapeutic drug targets, human indoleamine 2,3-dioxygenase and tryptophan dioxygenase, and (2) developing inhibitors targeting the enzymes as therapeutic strategies for cancer treatment. The postdoctoral fellow will join an exciting program with a focus on spectroscopy-guided crystallography, enzymology, and inhibitor design.
The successful applicant must have strong expertise in x-ray crystallography and optical spectroscopy, as well as hand-on experience in molecular cloning and protein purification. Additional training in computational modeling and/or molecular docking is a plus. Applicants should provide a CV and a cover letter justifying their suitability and interest in the position. Applicants should also arrange to have three letters of reference sent to Dr. Syun-Ru Yeh (syun-ru.yeh@einstein.yu.edu).
Albert Einstein College of Medicine is located in New York in a scenic Bronx campus that includes comfortable, affordable housing in an area rich with recreation and entertainment. The scientific environment provides outstanding research training opportunities.
A POSTDOCTORAL FELLOWSHIP position supported by The Welch Foundation is available immediately in the group of Prof. Francis Tsai in the Department of Biochemistry and Molecular Biology at Baylor College of Medicine in Houston, TX. The Tsai lab uses structural analysis techniques including X-ray crystallography, single-particle cryo-EM, and electron cryotomography (cryo-ET) to determine the structure, function, and mechanism of energy-dependent macromolecular machines involved in protein quality control and stress response signaling.
The successful applicant must be highly-motivated and possess demonstrated experience in protein biochemistry, gene cloning, and protein expression. Prior experience in enzymology or working with model organisms (bacteria, S. cerevisisae or C. elegans) is an advantage. Prior experience with structural analysis methods, including protein crystallography, NMR, or cryo-EM is not required and training will be provided as needed. Applicants should possess excellent written and verbal communication skills and have a recent Ph.D. in a relevant field. Salary is commensurate with experience and pegged to the current NIH scale.
We have an immediate opening for a talented, highly motivated postdoctoral fellow in my laboratory at the Ohio State University located in Columbus, Ohio. The research in our laboratory is mainly focused on understanding the role of cytoskeletal proteins in cell adhesion dynamics. We use multifaceted approach involving X-ray Crystallography, cryo-EM and cell biology to understand the mechanisms that dictate cell adhesion processes in health and disease.
We are looking for a postdoctoral candidate who is highly interested and motivated in the structure-function studies of macromolecular assemblies involved in cell adhesion. We expect that the successful candidate have demonstrated skills in structural biology (either cryo-EM or X-ray crystallography) and is willing to expand his/her skill set based on the demands of the project.
Review of applications will begin immediately and will continue until the position is filled. Interested applicants should send their CV along with a cover letter briefly describing their research accomplishments, current research interests and contact information for three references directly to Krishna.chinthalapudi@osumc.edu.
A technician position is available in the group Structural Biology of Novel Drug Targets in Human Diseases (Andrés Palencia, https://noveltargets-palencia.com), at the Institute for Advanced Biosciences (Grenoble) to work on the expression, purification of protein RNA complexes and co-crystallization with inhibitors in the area of infectious diseases.
In addition to structural biology and biophysical techniques, our laboratory also uses a wide range of approaches, from biochemistry and genetics to in vivo animal studies (in collaboration). We seek an outstanding candidate with training in molecular biology, protein biochemistry, with an interest in structural biology to support the study of novel protein drug targets.
The successful candidate will use the in-house IAB facilities and other structural biology facilities of the Partnership for Structural Biology in Grenoble (EMBL-IBS-ESRF-ILL, http://www.psb-grenoble.eu), and will have the opportunity to collaborate with industrial partners.
Applicants should possess experience in molecular biology and protein expression/purification by using bacterial, insect cell, or mammalian systems. Experience in RNA production, assembly and purification of protein-RNA complexes and crystallization would be an advantage. Motivation to work in a multidisciplinary and international environment is fundamental.
The candidate will work in the heart of the French Alpes (Grenoble) at the Institute for Advanced Biosciences (IAB), where creativity and excellence are fundamental to advance biomedical research and science education. The IAB is a research center of the University of Grenoble-Alpes, the French National Institute of Health and Medical Research (INSERM), and the French National Center for Scientific Research (CNRS). Grenoble provides access to state-of-the-art structural biology technologies available at the ESRF, EMBL, IBS and ILL. This includes new EM facilities equipped with Titan Krios, and Glacios/Falcon III. Other facilities include the ESRF synchrotron X-ray beamlines, high-field NMR at the IBS as well as the high-throughput crystallization platform at the EMBL, mammalian and insect cell facilities, and the biophysical platform. The lab has regular access to other synchrotrons: DLS, SOLEIL, and SLS.
Applicant should provide a motivation letter, a CV along with the contact information for two or more referees.
A Postdoctoral Scientist Position is available in the group Structural Biology of Novel Targets in Human Diseases (Andrés Palencia, https://noveltargets-palencia.com) at the Institute for Advanced Biosciences (Grenoble) to work on a drug discovery project in the area of infectious diseases, within the framework of the ANR project NovoTarget (2019–2023). This project consists of functional and structural characterization of new molecular targets and the investigation of the mechanism of action of inhibitors of these targets.
In addition to structural and biophysical techniques, our laboratory also uses a wide range of approaches, from biochemistry and genetics to in vivo animal studies (in collaboration). We seek an outstanding candidate with Ph.D. training in molecular and structural biology to study these novel protein drug targets.
The successful candidate will work on the production of protein and RNA samples and study it by using the in-house IAB facilities and other biophysical and structural biology facilities of the Partnership for Structural Biology in Grenoble (EMBL-IBS-ESRF-ILL, http://www.psb-grenoble.eu). The candidate will have the great opportunity to collaborate with industrial partners.
Applicants should possess a Ph.D. in structural biology (X-ray crystallography or electron microscopy), molecular biology or related, have a strong interest in drug discovery and a good publication record. Experience in bacterial, insect cell, or mammalian expression systems, as well as RNA production and purification of protein-RNA complexes would be an advantage. Excellent communication skills in English are needed for this job.
The candidate will work in the heart of the French Alpes (Grenoble) at the Institute for Advanced Biosciences (IAB), where creativity and excellence are fundamental to advance biomedical research and science education. The IAB is a research center of the University of Grenoble-Alpes, the French National Institute of Health and Medical Research (INSERM), and the French National Center for Scientific Research (CNRS). Grenoble provides access to state-of-the-art structural biology technologies available at the ESRF, EMBL, IBS and ILL. This includes new EM facilities equipped with Titan Krios and Glacios/Falcon III. Other facilities include the ESRF synchrotron X-ray beamlines, high-field NMR at the IBS as well as high-throughput crystallization platform at the EMBL, mammalian and insect cell facilities, and the biophysical platform. The lab has regular access to other synchrotrons: DLS, SOLEIL, DESY and SLS.
Applicant should provide a motivation letter, a CV along with the contact information for two or more referees, and a brief summary of current and previous research.
We have an opening for an enthusiastic post-doctoral fellow to study the molecular mechanisms governing actin polymerization, ATP hydrolysis, phosphate release, and filament stability in malaria parasite actins. The successful candidate has a keen interest to understand cytoskeletal proteins and cell motility in depth. A strong background in protein biochemistry and X-ray crystallography is required. Expertise in cryo-EM sample preparation and structure determination will be highly valued. In addition, a high level of own initiative and the ability to work in a team and supervise younger scientists are necessary.
The Faculty of Biochemistry and Molecular Medicine (FBMM; https://www.oulu.fi/fbmm/) is a dynamic and international working place, where the working language is English. Protein science is one of the focal areas of the Faculty. FBMM provides cutting-edge research facilities for molecular biology, protein biochemistry, X-ray crystallography, and light and electron microscopy. In addition, we have generous access to several large-scale facilities for structural biology (MX/SAXS/cryo-EM).
Funding is initially available for 2.5 years, but there may be possibilities for an extension. The starting date should be as soon as possible. Applications and informal enquiries should be sent by e-mail to inari.kursula@oulu.fi. Applications should contain (i) a cover letter detailing your specific interest in this project and your key skills and expertise, (ii) a CV including a list of publications, and (iii) contact information (e-mail) for 3 referees. Applications should preferably be sent by 30.4.2019, but screening of candidates will continue until a suitable one has been identified.
I have an immediate opening for the 2y industry sponsored PostDoc position in Structural Biology. The project is about membrane-embedded / membrane-associated enzymes.
Desirable skills: crystallisation / structure determination or experience in single-particle Cryo-EM.
Salary according to the collective labour agreement (cao) of Dutch Universities: level 10.4. Applicants from outside The Netherlands might be eligible for 30% tax deduction.
The Helmholtz Zentrum Berlin für Materialien und Energie, the Max-Delbrück-Center for Molecular Medicine, the Freie Universität Berlin, the Chariteand the Humboldt Universität zu Berlin jointly operate three experimental stations for bio-macromolecular crystallography at BESSY II, one of the world’s most modern synchrotron radiation sources for VUV and soft X-rays.
The Humboldt University zu Berlin is seeking a Post Doctoral Research Assistant to work on and support research topics in the field of structural enzymology (e.g. control of chemical reactions in macromolecular crystals, combination of UV/Vis absorption spectroscopy and crystallography, etc.) originating from the group of Prof. Dr. Holger Dobbek. The successful candidate will also be involved in the operation of the BESSY II bio-macromolecular crystallography beamlines (headed by Dr. Manfred S. Weiss) including supporting external users at the beamlines and will take part in graduate student education.
Initially, a contract lasting until 31.12.2020 will be offered to the successful candidate with the possibility for an extension. The salary will be based on German Federal TVöD. The position is available immediately.
Applicants should hold a Ph.D. in the biological, chemical or physical sciences and have a solid background in biochemical methods, in bio-macromolecular crystallography and/or related fields. The position also requires the documented ability to conduct independent research as well as excellent communication and interpersonal skills.
A research technician position is available in the laboratory of Dr. Karim-Jean Armache, Assistant Professor in the Structural Biology Program at the Skirball Institute of Biomedical Research—NYU Medical Center, New York, USA.
We are looking for creative individuals with a strong interest in protein and nucleic acid biochemistry. A commitment of at least 2 years is required. Ideal candidates should be highly motivated and have obtained a B.S. or M.S. degree with a background in biochemistry or molecular biology. Experience in molecular cloning and protein expression, as well as an ability to maintain organized records is essential. Experience with cell culture would be a plus. The candidate must have an excellent command of oral and written English. Applicants should send a single PDF file containing their CV along with a summary of their previous research experience, accomplishments, and experimental expertise.
The position is open immediately and applications will be reviewed until the position is filled.
at the Max Planck Institute for Medical Research, Heidelberg.
Virophages are small DNA viruses of unicellular eukaryotes that replicate only during a coinfection with a giant virus. They propagate at the expense of the giant virus using its cytosolic reproduction and assembly machinery. Virophages encode about 20 genes including two capsid proteins, a protease that assists maturation and a FtsK-HerA type ATPase that supposedly is responsible for ATP dependent DNA transport into the assembled capsid.
The successful candidates will characterize capsid assembly & processing and active DNA transport of the Virophage. The assembly/-disassembly pathway will be characterized with spectroscopic, kinetic and structural methods with the aim to better understand the hierarchy and pathway of supramolecular organisation of capsid structure and what determines the exact size of assembled particles in the absence of a molecular ruler.
Key to addressing these questions is the development and application of fluorescence based markers for FRET and Fluorescence Microscopy assays.
The gained knowledge will be used for recruiting in vitro assembled capsids for in vivo studies in collaboration with Matthias Fischer http://www.mpimf-heidelberg.mpg.de/14071687/gruppefischer.
The department has ample synchrotron beamtime at the SLS.
Successful candidates have an excellent track record, high motivation, and broad scienti?c interests. They will join a multidisciplinary international team. They should hold a master’s (Ph.D. or equivalent for postdoctoral candidates) degree in Biochemistry or related ?elds. The working language of the project will be English. We o?er excellent laboratory facilities tailored to the needs of the project. Payment is based on the TVöD guidelines.
Ph.D. candidates will have the opportunity to participate in one of several interdisciplinary Ph.D. programs in collaboration with the University of Heidelberg. The position is limited to three years with a possibility of extension.
For postdoctoral applicants, the position is limited to two years with a possibility of extension.
Please submit your application containing a cover letter (explaining background and motivation), your CV, complete transcripts (for Ph.D.
The Max Planck Society is committed to increasing the number of individuals with disabilities in its workforce and therefore encourages their application. The Max Planck Society strives for gender and diversity equality. We welcome applications from all backgrounds. A daycare center for children is located close to the institute.
here to advertise two postdoc positions in my lab at the Department of Biosciences, University of Milan, Italy.
The scientific project will deal on structural biology (Cryo-EM and crystallography) and biophysics of protein aggregation and amyloid fibril formation.
Specifically the projects will concentrate on two severe human pathologies: AL amyloidosis (a severe cardiac disorder) and on ALS (neurodegeneration).
Both projects will require a solid background in any of these disciplines: protein biochemistry, structural biology (crystallography or CryoEM), protein biophysics.
Specifically in both projects structural and biophysical characterisation of amyloidogenic proteins at the native state will be coupled with the inspection of the fibrillar assembly formed under pathologic conditions.
Selection will take place in the coming 2-3 months and contracts will start during summer (July - September).
A postdoctoral researcher position is available in the Zimmer lab at the University of Virginia School of Medicine. The lab explores how cells produce extracellular polysaccharides to form protective coats and capsules, cell walls, or biofilms.
Extracellular complex carbohydrates perform essential functions in all kingdoms of life and we strive to functionally reconstitute and structurally characterize various macromolecular complexes essential for their secretion. The lab has access to state-of-the-art cryo electron microscopy and X-ray crystallography facilities as well as single particle fluorescence and super-resolution light microscopes.
The University of Virginia has a particular strength in membrane biophysics and structural biology and is home to the Center for Membrane and Cell Physiology. The highly motivated candidate will join a diverse group working at the interface of structural and membrane biology, glycobiology, and biophysics. Candidates should have demonstrated expertise in cryo electron microscopy and/or crystallography, excellent skills in molecular biology and biochemistry, and at least one first author publication.
The University of Virginia is an equal opportunity employer. Applications from women and minorities are particularly welcome.
Interested candidates are encouraged to contact me directly by email for additional information (jz3x@virginia.edu).
The Fischer lab is recruiting a Staff Scientist for a project that exploits the protein conformational landscape for ligand discovery in pediatric cancer.
We are looking for applicants with a strong training in molecular biology, protein biochemistry, and structural biology and a keen interest or ideally experience in ligand discovery.
You will be part of a young, interdisciplinary team that uses structural biology (multi-temperature and high-throughput crystallography) to characterize disease-relevant protein states, computational methods to analyze and exploit them, and experiments (biophysical, biochemical, cell-based assays) to test the impact of small molecules on biology and disease. These approaches have relevance for allosteric regulation of proteins and protein-protein interactions.
1) Must be able to conduct independent research in molecular biology and protein biochemistry, including cloning and protein purification, that enable structural studies.
2) Demonstrated experience in protein crystallography.
3) Familiarity with large-scale/ high-throughput approaches, automation, liquid handling, biophysical assays or computational approaches is desirable.
4) Experience with expression systems other than E. coliand familiarity with cell-based assays is a plus.
5) Proficiency in e.g. python or shell scripting will facilitate scaling up data analysis.
6) Must be eager to learn and implement new techniques from those relevant areas.
support projects within the lab while maintaining efficient laboratory operations.
Our group is housed in the Department of Chemical Biology and Therapeutics (https://www.stjude.org/research/departments-divisions/chemical-biology-therapeutics.html), and Structural Biology (https://www.stjude.org/research/departments-divisions/structural-biology.html) at St. Jude Children’s Research Hospital. With ongoing investments into exceptional structural and chemical biology facilities, this is an exciting time to join our lab to do cutting-edge research whilst living in an affordable city.
Stable funding for this post is available.
A minimum of five (5) years of relevant and productive (combined) years postdoctoral research associate or five (5) years of combined academic experience at the postdoctoral level or above.
Please direct your questions and application package including a cover letter, current CV, and 3 letters of reference to: Dr. Marcus Fischer (marcus.fischer@stjude.org).
We have an immediate opening for a talented, highly motivated postdoctoral scholar in my laboratory at The University of Texas Medical Branch (UTMB) located in Galveston, TX (USA) to study the structure and function of ribosome functional complexes (https://microbiology.utmb.edu/faculty/matthieu-gagnon). The successful candidate will be involved in the characterization of prokaryotic and eukaryotic ribosomes, translation factors and other RNA/protein complexes. The research in our laboratory aims to elucidate the mechanisms of protein synthesis, antibiotic resistance and regulation of translation at a structural level using a combination of macromolecular X-ray crystallography, single-particle cryo-electron microscopy (cryo-EM) and biochemical techniques.
• Strong interest and motivation to elucidate the molecular mechanisms of protein synthesis and antibiotic resistance through structure determination.
The successful candidate will have an excellent track record and is expected to drive forward the projects, act independently or semi-independently, compile, analyze and write up data for publication, assist with the training of graduate students and work co-operatively with others.
Structural biology facilities at UTMB are outstanding (https://www.utmb.edu/core). Our cryo-electron microscopy (cryo-EM) core facility recently acquired the FEI Titan Krios high-voltage (300 kV) electron microscope equipped with two direct detector cameras, Falcon 3 (ThermoFisher) and K3 (Gatan), ideal setup for high-resolution structure visualization. Other cryo-EM resources include a JEOL 2200FS cryo-EM microscope equipped with a DE20 direct electron detector for high-resolution imaging work and a liquid nitrogen autofilling system allowing week-long experiments, a cryo-microscope JEOL 2100, an FEI vitrobot cryo-plunger, a Leica EM-GP2 cryo-plunger, a Gatan Solarus plasma cleaner. X-ray crystallography resources include two X-ray area detector systems, a Phoenix crystallization robot, a Minstrel crystal imaging robot, the Alchemist and epMotion liquid handling robots. Other state-of-the-art facilities include NMR, next-generation sequencing, molecular genomics, high-throughput screening, solution biophysics, optical microscopy and computational biology.
Ample opportunities exist at UTMB for interactions with centers of scientific excellence in structural biology and molecular biophysics, biodefense, molecular medicine, cancer biology, infectious diseases, environmental health, aging, and translational sciences (https://www.utmb.edu/centers). Moreover, UTMB boasts a renowned, vibrant and highly active community of infectious disease researchers and clinicians, providing ample opportunities for broader collaborations and development.
Review of applications will begin immediately and will continue until the position is filled. Interested applicants should send their CV along with a cover letter briefly describing their research accomplishments, current research interests and contact information for three references in a single PDF directly to Dr. Matthieu Gagnon at magagnon@utmb.edu.
We are seeking a highly motivated scientist for an EU-funded postdoctoral position in protein structural biology for an experimental team at Loschmidt Laboratories, Masaryk University, Brno, Czech Republic (https://loschmidt.chemi.muni.cz/peg/). We conduct basic research in enzymology and fight acute stroke, cancer and Alzheimer’s disease.
Perform protein expression, purification and biophysical characterization.
Design and perform protein crystallization experiments.
Collect X-ray diffraction data and determine protein-ligand complex structures.
Adapt emerging structural techniques: nanocrystallography and cryo-EM.
Work in a friendly, inspiring and highly collaborative environment.
Opportunities for further training, personal growth and benefits package.
PhD in structural biology, molecular biology, biochemistry or biophysics.
Experience with protein expression and purification.
Previous experience with protein structural techniques.
Experience with biophysical and biochemical protein characterization.
Willingness to learn new techniques: nanocrystallography and cryo-EM.
Ability to develop new concepts; goal-oriented and problem-solving skills.
Curriculum Vitae and motivation letter.