Preliminary X-ray Study of Naproxen Esterase from Bacillus subtilis

Single crystals of naproxen esterase from Bacillus subtilis have been obtained from PEG6000 solutions at pH 8·0 by liquid-liquid diffusion while applying a temperature gradient from 4°C to room temperature over a period of four weeks. The crystals belong to the trigonal space group P 3121 or P3221 w...

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Veröffentlicht in:	Journal of molecular biology 1993-03, Vol.230 (2), p.681-683
Hauptverfasser:	van der Laan, J.M., Teplyakov, A.V., Lammers, A.A., Dijkstra, B.W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacillus subtilis Bacillus subtilis - enzymology Bacteriology Biological and medical sciences Carboxylesterase Carboxylic Ester Hydrolases - chemistry Carboxylic Ester Hydrolases - isolation & purification Crystallization enantiomeric resolution esterase Fundamental and applied biological sciences. Psychology Metabolism. Enzymes Microbiology naproxen Protein Conformation X-Ray Diffraction - methods
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Beschreibung
Zusammenfassung:	Single crystals of naproxen esterase from Bacillus subtilis have been obtained from PEG6000 solutions at pH 8·0 by liquid-liquid diffusion while applying a temperature gradient from 4°C to room temperature over a period of four weeks. The crystals belong to the trigonal space group P 3121 or P3221 with a = b = 47·59 Å and c = 212·91 Å. The asymmetric part of the unit cell contains one protein molecule with Mr = 33,771. The crystals diffract to at least 3·0 Å resolution and are suitable for an X-ray structure analysis.
ISSN:	0022-2836 1089-8638
DOI:	10.1006/jmbi.1993.1184