Crystallization and preliminary X-ray analysis of a quadruple mutant of staphylococcal nuclease

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....

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Bibliographic Details
Published in:The Journal of biological chemistry 1988-12, Vol.263 (34), p.18190-18192
Main Authors: Loll, P J, Meeker, A K, Shortle, D, Pease, M, Lattman, E E
Format: Article
Language:English
Subjects:
Biological and medical sciences
Circular Dichroism
Crystalline structure
Crystallization
Fundamental and applied biological sciences. Psychology
Micrococcal Nuclease - genetics
Molecular biophysics
Mutation
Protein Conformation
ribonucleate(deoxyribonucleate) 3'-nucleotidohydrolase
Spectrometry, Fluorescence
Structure in molecular biology
X-Ray Diffraction
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)81343-1