Crystallization of a precursor penicillin acylase from Escherichia coli.
The crystallization of a mutant precursor penicillin acylase [penicillin amidohydrolase (amidase) E.C. 3.5.1.11] from Escherichia coli W (ATCC 11105) using the hanging-drop method is reported. The crystals are in space group P1 with unit-cell parameters a = 51.04, b = 63.58, c = 71.17 A, alpha = 103.0, beta = 110.6, gamma = 105.3 degrees, with one molecule in the asymmetric unit, and diffract to 1. 8 A using synchrotron radiation.
Hewitt
L
L
Department of Chemistry, University of York, Heslington, York YO1 5DD, England. lol@yorvic.york.ac.uk
Kasche
V
V
Lummer
K
K
Rieks
A
A
Wilson
K S
KS
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D009154:Mutation; D010399:Penicillin Amidase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D001426:Bacterial Proteins; D010399:Penicillin Amidase