Disordered water within a hydrophobic protein cavity visualized by x-ray crystallography.

ABSTRACT: Water in the hydrophobic cavity of human interleukin 1beta, which was detected by NMR spectroscopy but was invisible by high resolution x-ray crystallography, has been mapped quantitatively by measurement and phasing of all of the low resolution x-ray diffraction data from a single crystal. Phases for the low resolution data were refined by iterative density modification of an initial flat solvent model outside the envelope of the atomic model. The refinement was restrained by the condition that the map of the difference between the electron density distribution in the full unit cell and that of the atomic model be flat within the envelope of the well ordered protein structure. Care was taken to avoid overfitting the diffraction data by maintaining phases for the high resolution data from

SUBMITTER: Yu B 

PROVIDER: S-EPMC15100 | biostudies-literature | 1999 Jan

REPOSITORIES: biostudies-literature