1ja2
From Proteopedia
BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: A POWDER DIFFRACTION STUDY
Overview
The binding of N-acetylglucosamine (NAG) to chicken egg lysozyme (E.C. 3.2.1.17) was investigated by high-resolution X-ray powder diffraction at room temperature. NAG was found to bind to lysozyme in a rapid precipitation preparation with 0.05 M NaCl buffer pH 6.0, but not 0.05 M NaCl buffer pH 5.0. Binding was indicated by significant and readily apparent changes in the diffraction pattern from that of the apo protein precipitated from the same solvent. The location of NAG bound to lysozyme was easily found from a difference Fourier map generated from structure factors extracted during a preliminary combined Rietveld and stereochemical restraint refinement. Full protein and protein-NAG structures were refined with these techniques (R(wp) = 2.22-2.49%, R(p) = 1.79-1.95%, R(F)(2) = 4.95-6.35%) and revealed a binding mode for NAG which differed from that found in an earlier single-crystal study and probably represents a precursor trapped by rapid precipitation.
About this Structure
1JA2 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Binding of N-acetylglucosamine to chicken egg lysozyme: a powder diffraction study., Von Dreele RB, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1836-42. Epub 2001, Nov 21. PMID:11717496 Page seeded by OCA on Fri May 2 20:58:01 2008
