Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystallization and preliminary X-ray analysis of a gamma-lactamase.,Gonsalvez IS, Isupov MN, Littlechild JA Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):284-6. PMID:11173481[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gonsalvez IS, Isupov MN, Littlechild JA. Crystallization and preliminary X-ray analysis of a gamma-lactamase. Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):284-6. PMID:11173481
