1lzn
From Proteopedia
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NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME
Overview
Triclinic crystals of lysozyme, hydrogen-deuterium exchanged in deuterated, solvent, have been studied using neutron quasi-Laue techniques and a newly, developed cylinder image-plate detector. The wavelength range employed was, from 2.7 to 3.5 A, which gave 9426 significant reflections [F >/=, 2sigma(F)] to a resolution limit of 1. 7 A. The deuteration states of the, H atoms in the protein molecule were identified, followed by an extensive, analysis of the water structure surrounding the protein. The final R, factor was 20.4% (Rfree = 22.1%). In total, the 244 observed water, molecules form approximately one layer of water around the protein with, far fewer water molecules located further away. Water molecules covering, the apolar patches make tangential layers at 4-5 A from the surface or, form C-H...O contacts, and several water-molecule sites can be identified, in the apolar cavities. Many of the water molecules are apparently, orientationally disordered, and only 115 out of the 244 water molecules, sit in mean single orientations. Comparison of these results with, quasi-elastic neutron scattering observations of the water dynamics leads, to a picture of the water molecules forming an extended constantly, fluctuating network covering the protein surface.
About this Structure
1LZN is a Single protein structure of sequence from Gallus gallus with NO3, NA and DOD as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Quasi-Laue neutron-diffraction study of the water arrangement in crystals of triclinic hen egg-white lysozyme., Bon C, Lehmann MS, Wilkinson C, Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):978-87. PMID:10216294
Page seeded by OCA on Tue Nov 20 21:00:50 2007
Categories: Gallus gallus | Lysozyme | Single protein | Bon, C.I. | Lehmann, M.S. | Wilkinson, C. | DOD | NA | NO3 | Hydrolase
