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

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Abstract

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.

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Gonsalvez, I. S., Isupov, M. N., & Littlechild, J. A. (2001). Crystallization and preliminary X-ray analysis of a γ-lactamase. Acta Crystallographica Section D: Biological Crystallography, 57(2), 284–286. https://doi.org/10.1107/S0907444900016838

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