1io5
From Proteopedia
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HYDROGEN AND HYDRATION OF HEN EGG-WHITE LYSOZYME DETERMINED BY NEUTRON DIFFRACTION
Overview
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.
About this Structure
1IO5 is a Single protein structure of sequence from Gallus gallus with DOD as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 17:32:19 2007
Categories: Gallus gallus | Lysozyme | Single protein | Castagna, J.C. | Cipriani, F. | Hoeghoej, P. | Lehmann, M.S. | Minezaki, Y. | Niimura, N. | Nonaka, T. | Wilkinson, C. | DOD | Hydration | Hydrogen | Hydrolase
