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Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans.

P L Roach·C J Schofield·J E Baldwin·I J Clifton·J Hajdu
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Abstract

Recombinant Aspergillus nidulans isopenicillin N synthase was purified from an Escherichia coli expression system. The apoenzyme in the presence of saturating concentrations of MnCl2 could be crystallized by either macro- or microseeding, using the hanging drop vapor diffusion technique with polyethylene glycol 8000 as precipitant. The crystals (0.5-1.0 mm overall dimensions) diffract X-rays to at least 2.0 A resolution at synchrotrons and belong to space group P212121 with unit cell dimensions of a = 59.2 A, b = 127.0 A, and c = 139.6 A. The asymmetric unit contains one dimer, and the solvent content of the crystals is 60%. The crystals are radiation sensitive.

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Aspergillus nidulansCrystallizationCrystallography, X-RayMolecular StructureOxidoreductasesPolyethylene GlycolsProtein ConformationRecombinant ProteinsJournal ArticleResearch Support, Non-U.S. Gov't

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P L Roach, C J Schofield, J E Baldwin, I J Clifton, J Hajdu. 1995. Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans.. https://doi.org/10.1002/pro.5560040521

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