1io5 | pdb_00001io5

HYDROGEN AND HYDRATION OF HEN EGG-WHITE LYSOZYME DETERMINED BY NEUTRON DIFFRACTION

spinqualitylabelsall models 1io5, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1io5 is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Neutron Diffraction, Resolution 2Å Ligands: DOD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LYSC_CHICK Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Neutron quasi-Laue diffraction data (2 A resolution) from tetragonal hen egg-white lysozyme were collected in ten days with neutron imaging plates. The data processing Laue software, LAUEGEN, developed for X-ray Laue diffractometry, was adapted for neutron diffractometry with a cylindrical detector. The data analysis software, X-PLOR, was modified and used for the refinement of hydrogen atoms, and the positions of 960 hydrogen atoms in the protein and 157 bound water molecules, were determined. Several examples are given of the methods used to identify hydrogen atoms and water molecules. Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography.,Niimura N, Minezaki Y, Nonaka T, Castagna JC, Cipriani F, Hoghoj P, Lehmann MS, Wilkinson C Nat Struct Biol. 1997 Nov;4(11):909-14. PMID:9360606 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysozyme 3D structures

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