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Crystallization and preliminary X-ray diffraction studies of recombinant human ornithine aminotransferase.
J Mol Biol. 1994 Oct 14; 243(1):128-30.JM

Abstract

Human liver ornithine aminotransferase was expressed in Escherichia coli and purified by ammonium sulfate fractionation and anion exchange column chromatography. The purified recombinant enzyme is fully active and crystallized readily over a wide range of polyethylene glycol concentrations. The crystals belong to the trigonal space group P3(1)21 (or its enantiomorph P3(2)21) with unit cell parameters a = b = 116.3 A, and c = 190.0 A, alpha = beta = 90 degrees, gamma = 120 degrees. There are three monomers per asymmetric unit. Self-rotation function studies revealed both 2-fold and 3-fold non-crystallographic symmetry, with the local 3-fold axis being tilted 15 degrees from the c axis and perpendicular to a crystallographic dyad. A complete native data set to 2.3 A resolution was collected using synchrotron radiation.

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Authors+Show Affiliations

Shen BW
Chemistry Department, Purdue University, W. Lafayette, IN.
Ramesh V
No affiliation info available
Mueller R
No affiliation info available
Hohenester E
No affiliation info available
Hennig M
No affiliation info available
Jansonius JN
No affiliation info available

MeSH

Cloning, MolecularCrystallizationCrystallography, X-RayEscherichia coliHumansOrnithine-Oxo-Acid TransaminaseRecombinant Proteins

Pub Type(s)

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

Language

eng

PubMed ID

7932736

Citation

Shen, B W., et al. "Crystallization and Preliminary X-ray Diffraction Studies of Recombinant Human Ornithine Aminotransferase." Journal of Molecular Biology, vol. 243, no. 1, 1994, pp. 128-30.
Shen BW, Ramesh V, Mueller R, et al. Crystallization and preliminary X-ray diffraction studies of recombinant human ornithine aminotransferase. J Mol Biol. 1994;243(1):128-30.
Shen, B. W., Ramesh, V., Mueller, R., Hohenester, E., Hennig, M., & Jansonius, J. N. (1994). Crystallization and preliminary X-ray diffraction studies of recombinant human ornithine aminotransferase. Journal of Molecular Biology, 243(1), 128-30.
Shen BW, et al. Crystallization and Preliminary X-ray Diffraction Studies of Recombinant Human Ornithine Aminotransferase. J Mol Biol. 1994 Oct 14;243(1):128-30. PubMed PMID: 7932736.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray diffraction studies of recombinant human ornithine aminotransferase. AU - Shen,B W, AU - Ramesh,V, AU - Mueller,R, AU - Hohenester,E, AU - Hennig,M, AU - Jansonius,J N, PY - 1994/10/14/pubmed PY - 1994/10/14/medline PY - 1994/10/14/entrez SP - 128 EP - 30 JF - Journal of molecular biology JO - J Mol Biol VL - 243 IS - 1 N2 - Human liver ornithine aminotransferase was expressed in Escherichia coli and purified by ammonium sulfate fractionation and anion exchange column chromatography. The purified recombinant enzyme is fully active and crystallized readily over a wide range of polyethylene glycol concentrations. The crystals belong to the trigonal space group P3(1)21 (or its enantiomorph P3(2)21) with unit cell parameters a = b = 116.3 A, and c = 190.0 A, alpha = beta = 90 degrees, gamma = 120 degrees. There are three monomers per asymmetric unit. Self-rotation function studies revealed both 2-fold and 3-fold non-crystallographic symmetry, with the local 3-fold axis being tilted 15 degrees from the c axis and perpendicular to a crystallographic dyad. A complete native data set to 2.3 A resolution was collected using synchrotron radiation. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/7932736/Crystallization_and_preliminary_X_ray_diffraction_studies_of_recombinant_human_ornithine_aminotransferase_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(84)71637-8 DB - PRIME DP - Unbound Medicine ER -