Publication Abstract from PubMed
Tetragonal crystals of hen egg white lysozyme were cross-linked and subjected to X-ray diffraction study in acetonitrile-water media with different acetonitrile concentrations. Crystals in neat acetonitrile did not scatter X-ray well. Structures of crystals in neat water, in 90% and 95% acetonitrile, and crystal back-soaked from acetonitrile to water, were determined to about 2 A resolution. For crystals in both 90% acetonitrile, and crystal back-soaked from acetonitrile to water, were determined to about 2 A resolution. For crystals in both 90% and 95% acetonitrile, only one protein-bond acetonitrile molecule is found in the active site cleft, and its location and binding-protein mode is similar to the C subunit of polysaccharide. The alteration in conformation and hydrogen-bond pattern involving water as solvent causes the reduction of the protein's flexibility in organic media. The back-soaked crystal regained its ordinary three-dimensional structure in water.
X-ray studies on cross-linked lysozyme crystals in acetonitrile-water mixture.,Wang Z, Zhu G, Huang Q, Qian M, Shao M, Jia Y, Tang Y Biochim Biophys Acta. 1998 May 19;1384(2):335-44. PMID:9659395[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
