4lyo
From Proteopedia
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CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN NEAT ACETONITRILE, THEN BACK-SOAKED IN WATER
Overview
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.
About this Structure
4LYO is a Single protein structure of sequence from Gallus gallus. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 19:13:42 2008
Categories: Gallus gallus | Lysozyme | Single protein | Huang, Q. | Jia, Y. | Qian, M. | Shao, M. | Tang, Y. | Wang, Z. | Zhu, G. | Cross-linked | Hydrolase | Hydrolase (o-glycosyl)
