Crystallization and preliminary diffraction analysis of an engineered cephalosporin acylase.
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.
Anandan
Anandhi
A
School of Biomedical, Biomolecular and Chemical Sciences, University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia.
Vallet
Corinne
C
Coyle
Travis
T
Moustafa
Ibrahim M
IM
Vrielink
Alice
A
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
D011994:Recombinant Proteins; D010399:Penicillin Amidase