Crystallization and preliminary X-ray analysis of a γ-­lactamase

An enzyme from Comomonas acidovorans has been isolated that is specific for the stereospecific hydrolysis of (+)γ‐lactam. This so‐called (+)γ‐lactamase has important applications in biotransformation reactions. The enzyme has been crystallized by vapour‐phase diffusion using polyethylene glycol 4000...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-02, Vol.57 (2), p.284-286
Main Authors: Gonsalvez, Irene S., Isupov, Michail N., Littlechild, Jennifer A.
Format: Article
Language:English
Subjects:
Amidohydrolases - chemistry
Amidohydrolases - isolation & purification
Amidohydrolases - metabolism
Betaproteobacteria - enzymology
Crystallization
Crystallography, X-Ray
Enzyme Inhibitors - pharmacology
lactamases
Mass Spectrometry
Polyethylene Glycols
Sequence Alignment
Sequence Homology, Amino Acid
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Summary:An enzyme from Comomonas acidovorans has been isolated that is specific for the stereospecific hydrolysis of (+)γ‐lactam. This so‐called (+)γ‐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, β‐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 Å, α = 104.3, β = 92.6, γ = 108.5°, and diffract to 2 Å resolution using synchrotron radiation. Native data from these crystals have been collected to 2.4 Å.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444900016838