期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 57, 期 -, 页码 284-286出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444900016838
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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 Angstrom, alpha = 104.3, beta = 92.6, gamma = 108.5 degrees, and diffract to 2 Angstrom resolution using synchrotron radiation. Native data from these crystals have been collected to 2.4 Angstrom.
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