Protein Engineering, Vol. 12, No. 12, 1021-1024,
December 1999
© 1999 Oxford University Press
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Correlation between occupancy and B factor of water molecules in protein crystal structures
European Molecular Biology Laboratory, Meyerhofstrasse 1,69012 Heidelberg, Germany and Department of General Chemistry,Pavia University, via Taramelli 12, 27100 Pavia, Italy.E-mail: carugo{at} embl-heidelberg.de
An empirical relationship between occupancy and the atomic displacement parameter of water molecules in protein crystal structures has been found by comparing a set of well refined sperm whale myoglobin crystal structures. The relationship agrees with a series of independent structural features whose impact on water occupancy can easily be predicted as well as with other known data and is independent of the protein fold. The estimation of the water occupancy in protein crystal structures may help in understanding the physico-chemical properties of the protein–solvent interface and can allow the monitoring of the accuracy of the protein crystal structure refinement.
Keywords: atomic displacement parameter/occupancy/protein hydration/protein structure/water structure
1 Correspondence should be sent to the Pavia address
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