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Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans.
Protein Sci. 1995 May; 4(5):1007-9.PS

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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Authors+Show Affiliations

Roach PL
Dyson Perrins Laboratory, University of Oxford, United Kingdom.
Schofield CJ
No affiliation info available
Baldwin JE
No affiliation info available
Clifton IJ
No affiliation info available
Hajdu J
No affiliation info available

MeSH

Aspergillus nidulansCrystallizationCrystallography, X-RayMolecular StructureOxidoreductasesPolyethylene GlycolsProtein ConformationRecombinant Proteins

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

7663335

Citation

Roach, P L., et al. "Crystallization and Preliminary X-ray Diffraction Studies On Recombinant Isopenicillin N Synthase From Aspergillus Nidulans." Protein Science : a Publication of the Protein Society, vol. 4, no. 5, 1995, pp. 1007-9.
Roach PL, Schofield CJ, Baldwin JE, et al. Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans. Protein Sci. 1995;4(5):1007-9.
Roach, P. L., Schofield, C. J., Baldwin, J. E., Clifton, I. J., & Hajdu, J. (1995). Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans. Protein Science : a Publication of the Protein Society, 4(5), 1007-9.
Roach PL, et al. Crystallization and Preliminary X-ray Diffraction Studies On Recombinant Isopenicillin N Synthase From Aspergillus Nidulans. Protein Sci. 1995;4(5):1007-9. PubMed PMID: 7663335.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans. AU - Roach,P L, AU - Schofield,C J, AU - Baldwin,J E, AU - Clifton,I J, AU - Hajdu,J, PY - 1995/5/1/pubmed PY - 1995/5/1/medline PY - 1995/5/1/entrez SP - 1007 EP - 9 JF - Protein science : a publication of the Protein Society JO - Protein Sci VL - 4 IS - 5 N2 - 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. SN - 0961-8368 UR - https://www.unboundmedicine.com/medline/citation/7663335/Crystallization_and_preliminary_X_ray_diffraction_studies_on_recombinant_isopenicillin_N_synthase_from_Aspergillus_nidulans_ L2 - https://doi.org/10.1002/pro.5560040521 DB - PRIME DP - Unbound Medicine ER -