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J Struct Biol. 1996 Jul-Aug;117(1):73-6.

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

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1
Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany.

Abstract

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.

PMID:
8776890
DOI:
10.1006/jsbi.1996.0071
[Indexed for MEDLINE]

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