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B6db references: 95018246

type Journal Article
authors Shen, B. W.; Ramesh, V.; Mueller, R.; Hohenester, E.; Hennig, M.; Jansonius, J. N.
title Crystallization and preliminary X-ray diffraction studies of recombinant human ornithine aminotransferase
journal J Mol Biol
ui 95018246
year (1994)
volume 243
number 1
pages 128-30.
keywords Cloning, Molecular
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.
last changed 2002/11/04 17:41

B6db references