Crystallization and preliminary X-ray analysis of cephalosporin C acylase from Pseudomonas sp. strain N176.
Cephalosporin C acylase from Pseudomonas sp. strain N176, a heterodimer of 25 and 58 kDa, has been crystallized using polyethylene glycol 6000 as precipitant. The crystals are orthorhombic and have unit-cell parameters a = 141.41, b = 192.10, c = 80.75 A. They belong to space group P2(1)2(1)2(1) and diffract to at least 2.7 A resolution. Calculations indicate that there are two heterodimers in the asymmetric unit. The structure is being solved by molecular replacement using penicillin G acylase from Escherichia coli as a search model and by multiple isomorphous replacement.
Kinoshita
T
T
Basic Research Laboratories, Fujisawa Pharmaceutical Co. Ltd, 1-6 Kashima 2-Chome, Yodogawa-ku, Osaka 532-8514, Japan. takayoshi_kinoshita@po.fujisawa.co.jp
Tada
T
T
Saito
Y
Y
Ishii
Y
Y
Sato
A
A
Murata
M
M
D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology; D010399:Penicillin Amidase / Q000737:chemistry* / Q000302:isolation & purification; D011549:Pseudomonas / Q000201:enzymology*
D010399:Penicillin Amidase