title: Crystallization and preliminary diffraction analysis of an engineered cephalosporin acylase.
abstract: Crystallization conditions are reported for an engineered cephalosporin acylase based on the sequence of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas strain N176. Initial crystals were grown using polyethylene glycol as a crystallizing agent; however, these crystals diffracted poorly and exhibited high mosaicity. A dehydration procedure in which crystals were transferred to a solution containing a higher concentration of polyethylene glycol as well as glycerol improved the diffraction quality such that a 1.57 A diffraction data set could be obtained.
authors.affiliation: School of Biomedical, Biomolecular and Chemical Sciences, University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia.
authors.forename: Anandhi
authors.initials: A
authors.lastname: Anandan
authors.forename: Corinne
authors.initials: C
authors.lastname: Vallet
authors.forename: Travis
authors.initials: T
authors.lastname: Coyle
authors.forename: Ibrahim M
authors.initials: IM
authors.lastname: Moustafa
authors.forename: Alice
authors.initials: A
authors.lastname: Vrielink
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D009154:Mutation; D010399:Penicillin Amidase / Q000737:chemistry* / Q000235:genetics; D011549:Pseudomonas / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D011994:Recombinant Proteins; D010399:Penicillin Amidase