1LYO

CROSS-LINKED LYSOZYME CRYSTAL IN NEAT WATER

Summary for 1LYO

• Entry DOI: 10.2210/pdb1lyo/pdb
• Descriptor: LYSOZYME (2 entities in total)
• Functional Keywords: hydrolase (o-glycosyl), hydrolase, lysozyme, cross-linked
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14331.16

Authors

Huang, Q.,Wang, Z.,Zhu, G.,Qian, M.,Shao, M.,Jia, Y.,Tang, Y. (deposition date: 1998-03-05, release date: 1998-05-27, Last modification date: 2023-08-09)

Primary citation

Wang, Z.,Zhu, G.,Huang, Q.,Qian, M.,Shao, M.,Jia, Y.,Tang, Y.
X-ray studies on cross-linked lysozyme crystals in acetonitrile-water mixture.
Biochim.Biophys.Acta, 1384:335-344, 1998

PubMed Abstract: 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.

PubMed: 9659395
DOI: 10.1016/S0167-4838(98)00027-2

Experimental method

X-RAY DIFFRACTION (1.93 Å)