Crystallization and preliminary high-resolution X-ray diffraction analysis of native and β-mercaptoethanol-inhibited urease from Bacillus pasteurii
- 1 May 1998
- journal article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 54 (3) , 409-412
- https://doi.org/10.1107/s0907444997013085
Abstract
Hexagonal crystals of urease from Bacillus pasteurii have been obtained by vapour diffusion at 293 K in 20 mM Tris–HCl, neutral pH, containing 50 mM Na2SO3. Isomorphous crystals of urease inhibited with β-mercaptoethanol were also obtained by including 4 mM of the inhibitor in the enzyme solution. Crystals of the native and inhibited enzyme diffract, respectively, to 2.00 Å (96.7% completeness) and to 1.65 Å (98.7% completeness) using synchrotron X-ray cryogenic (100 K) conditions. The space group is P6322 for both forms, and the unit-cell parameters are a = b = 131.36, c = 189.76 Å for native urease and a = b = 131.34, c = 190.01 Å for inhibited urease. Under the same conditions, single crystals of B. pasteurii urease inhibited with acetohydroxamic acid, cisteamine, and phenylphosphorodiamidate were also obtained.Keywords
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