Crystallization and preliminary X-ray diffraction analysis of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae

Crystallization and preliminary X-ray diffraction analysis of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae

Single crystals of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae have been grown by vapor diffusion using phosphate buffer as the precipitant. The crystals belong to the monoclinic space group C2 with a = 86.9 A, b = 155.9 A, c = 83.8 A, beta = 91.6 degrees. Assuming two mon...

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Veröffentlicht in:Journal of structural biology 1996-07, Vol.117 (1), p.73-76
Hauptverfasser: Sack, S, Dauter, Z, Wanke, C, Amrhein, N, Mandelkow, E, Schönbrunn, E
Format: Artikel
Sprache:eng
Schlagworte:
Alkyl and Aryl Transferases
Crystallization
Crystallography, X-Ray
Enterobacter cloacae - enzymology
Protein Conformation
Recombinant Proteins - chemistry
Transferases - chemistry
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Zusammenfassung:Single crystals of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae have been grown by vapor diffusion using phosphate buffer as the precipitant. The crystals belong to the monoclinic space group C2 with a = 86.9 A, b = 155.9 A, c = 83.8 A, beta = 91.6 degrees. Assuming two monomers per asymmetric unit, the solvent content of these crystals is 63%. Flash-frozen crystals diffract to beyond 2 A resolution.
ISSN:1047-8477
DOI:10.1006/jsbi.1996.0071