Crystallization and preliminary X-ray analysis of a quadruple mutant of staphylococcal nuclease.
P. J. Loll, A. K. Meeker, D. Shortle, M. Pease, E. E. Lattman
A quadruple mutant of staphylococcal nuclease, nuclease (V66L/G79S/G88V/L108V), has been crystallized in a form well suited to moderate-to-high resolution x-ray diffraction analysis. This mutant is highly unstable; only about 20% of the protein in solution at room temperature is in its folded form. Under the crystallization conditions, the protein exhibits circular dichroism properties similar to, but not identical with, those of native wild type protein. The crystals belong to the space group P6(1)22 or P6(5)22 with unit cell dimensions of a = b = 61.1 A, c = 170.1 A and diffract to at least 2.5 A resolution. A data set complete to 3.7 A resolution has been collected and processed; attempts to determine the structure using molecular replacement techniques are under way.
The Journal of biological chemistry
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Micrococcal Nuclease Medicine & Life Sciences 100%
Crystallization Medicine & Life Sciences 82%
X-Rays Medicine & Life Sciences 53%
Molecular Replacement Chemical Compounds 28%
Circular Dichroism Medicine & Life Sciences 28%
Molecular Structure Medicine & Life Sciences 27%
Loll, P. J., Meeker, A. K., Shortle, D., Pease, M., & Lattman, E. E. (1988). Crystallization and preliminary X-ray analysis of a quadruple mutant of staphylococcal nuclease. The Journal of biological chemistry, 263(34), 18190-18192.
Crystallization and preliminary X-ray analysis of a quadruple mutant of staphylococcal nuclease. / Loll, P. J.; Meeker, A. K.; Shortle, D. et al.
In: The Journal of biological chemistry, Vol. 263, No. 34, 05.12.1988, p. 18190-18192.
Loll, PJ, Meeker, AK, Shortle, D, Pease, M & Lattman, EE 1988, 'Crystallization and preliminary X-ray analysis of a quadruple mutant of staphylococcal nuclease.', The Journal of biological chemistry, vol. 263, no. 34, pp. 18190-18192.
Loll PJ, Meeker AK, Shortle D, Pease M, Lattman EE. Crystallization and preliminary X-ray analysis of a quadruple mutant of staphylococcal nuclease. The Journal of biological chemistry. 1988 Dec 5;263(34):18190-18192.
Loll, P. J. ; Meeker, A. K. ; Shortle, D. et al. / Crystallization and preliminary X-ray analysis of a quadruple mutant of staphylococcal nuclease. In: The Journal of biological chemistry. 1988 ; Vol. 263, No. 34. pp. 18190-18192.
@article{060da752b1f9484b819d23b1c1faece5,
title = "Crystallization and preliminary X-ray analysis of a quadruple mutant of staphylococcal nuclease.",
abstract = "A quadruple mutant of staphylococcal nuclease, nuclease (V66L/G79S/G88V/L108V), has been crystallized in a form well suited to moderate-to-high resolution x-ray diffraction analysis. This mutant is highly unstable; only about 20% of the protein in solution at room temperature is in its folded form. Under the crystallization conditions, the protein exhibits circular dichroism properties similar to, but not identical with, those of native wild type protein. The crystals belong to the space group P6(1)22 or P6(5)22 with unit cell dimensions of a = b = 61.1 A, c = 170.1 A and diffract to at least 2.5 A resolution. A data set complete to 3.7 A resolution has been collected and processed; attempts to determine the structure using molecular replacement techniques are under way.",
author = "Loll, {P. J.} and Meeker, {A. K.} and D. Shortle and M. Pease and Lattman, {E. E.}",
note = "Copyright: This record is sourced from MEDLINE{\textregistered}/PubMed{\textregistered}, a database of the U.S. National Library of Medicine",
journal = "Journal of Biological Chemistry",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
T1 - Crystallization and preliminary X-ray analysis of a quadruple mutant of staphylococcal nuclease.
AU - Loll, P. J.
AU - Meeker, A. K.
AU - Shortle, D.
AU - Pease, M.
AU - Lattman, E. E.
N1 - Copyright: This record is sourced from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
N2 - A quadruple mutant of staphylococcal nuclease, nuclease (V66L/G79S/G88V/L108V), has been crystallized in a form well suited to moderate-to-high resolution x-ray diffraction analysis. This mutant is highly unstable; only about 20% of the protein in solution at room temperature is in its folded form. Under the crystallization conditions, the protein exhibits circular dichroism properties similar to, but not identical with, those of native wild type protein. The crystals belong to the space group P6(1)22 or P6(5)22 with unit cell dimensions of a = b = 61.1 A, c = 170.1 A and diffract to at least 2.5 A resolution. A data set complete to 3.7 A resolution has been collected and processed; attempts to determine the structure using molecular replacement techniques are under way.
AB - A quadruple mutant of staphylococcal nuclease, nuclease (V66L/G79S/G88V/L108V), has been crystallized in a form well suited to moderate-to-high resolution x-ray diffraction analysis. This mutant is highly unstable; only about 20% of the protein in solution at room temperature is in its folded form. Under the crystallization conditions, the protein exhibits circular dichroism properties similar to, but not identical with, those of native wild type protein. The crystals belong to the space group P6(1)22 or P6(5)22 with unit cell dimensions of a = b = 61.1 A, c = 170.1 A and diffract to at least 2.5 A resolution. A data set complete to 3.7 A resolution has been collected and processed; attempts to determine the structure using molecular replacement techniques are under way.
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry