Crystallization and preliminary X-ray analysis of a gamma-lactamase.
An enzyme from Comomonas acidovorans has been isolated that is specific for the stereospecific hydrolysis of (+)gamma-lactam. This so-called (+)gamma-lactamase has important applications in biotransformation reactions. The enzyme has been crystallized by vapour-phase diffusion using polyethylene glycol 4000 as a precipitant. Addition of a detergent, beta-octylglucoside, was found to be essential for obtaining diffraction-quality crystals. The crystals grow in the space group P1, with unit-cell parameters a = 63.0, b = 93.2, c = 152.4 A, alpha = 104.3, beta = 92.6, gamma = 108.5 degrees, and diffract to 2 A resolution using synchrotron radiation. Native data from these crystals have been collected to 2.4 A.
Gonsalvez
I S
IS
School of Chemistry, University of Exeter, Exeter EX4 4QD, England.
Isupov
M N
MN
Littlechild
J A
JA
D000581:Amidohydrolases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D020562:Betaproteobacteria / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000494:pharmacology; D013058:Mass Spectrometry; D011092:Polyethylene Glycols; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D004791:Enzyme Inhibitors; D011092:Polyethylene Glycols; D000581:Amidohydrolases; C401943:gamma-lactamase