Article
Crystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product.
Journal of molecular biology - 11 Nov 1994
Hadfield A T, Harvey D J, Archer D B, MacKenzie D A, Jeenes D J, Radford S E, Lowe G, Dobson C M, Johnson L N
Abstract excerpt
The crystal structure of a mutant hen egg white lysozyme, in which the key catalytic residue aspartic acid 52 has been changed to a serine residue (D52S HEWL), has been determined and refined to a crystallographic R value of 0.173 for all data F > 0 between 8 and 1.9 A resolution. The D52S HEWL structure is very similar to the native HEWL structure (r.m.s. deviation of main-chain atoms 0.20 A). Small shifts that...
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