Incorporation of crystallographic temperature factors in the statistical analysis of protein tertiary structures

A method to identify statistically significant differences between equivalent atoms in two closely related protein X-ray crystallographic structures is described. This method uses the linear relationship found between the logarithm of the distance between equivalent atoms and their mean temperature...

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Bibliographic Details
Published in:Protein engineering 1990-08, Vol.3 (8), p.649-657
Main Authors: Bott, Richard, Frane, James
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Cattle
Chymotrypsin - chemistry
Crystalline structure
Fundamental and applied biological sciences. Psychology
Molecular biophysics
Muramidase - chemistry
Phospholipases A - chemistry
Protein Conformation
Regression Analysis
site-specific variant structure
Structure in molecular biology
Subtilisins - chemistry
Temperature
Trypsin - chemistry
X-ray crystallography
X-Ray Diffraction
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Summary:A method to identify statistically significant differences between equivalent atoms in two closely related protein X-ray crystallographic structures is described. This method uses the linear relationship found between the logarithm of the distance between equivalent atoms and their mean temperature factor to determine, by linear regression, the expected difference and variance.
ISSN:1741-0126
0269-2139
1741-0134
1460-213X
DOI:10.1093/protein/3.8.649