Title: Crystallization and initial X-ray diffraction analysis of the tellurite-resistance S-adenosyl-L-methionine transferase protein TehB from Escherichia coli. | Journal: Acta crystallographica. Section F, Structural biology and crystallization communications. 2010 Nov;66(Pt 11):1496-9 | Authors: Choudhury HG, Beis K. | Abstract: TehB is an S-adenosyl-L-methionine (SAM) dependent methyltransferase that detoxifies tellurite in bacteria. The Escherichia coli TehB protein was purified and crystallized in the presence of both SAM and sinefungin. The TehB-SAM and TehB-sinefungin crystals both diffracted X-rays to 1.9 Å resolution. The TehB-SAM crystals belonged to space group C2, with unit-cell parameters a = 60.0, b = 56.1, c = 130.6 Å, β = 97.9°. The TehB-sinefungin crystals belonged to space group P2(1), with unit-cell parameters a = 59.1, b = 55.5, c = 129.7 Å, β = 95.9°. | See full PubMed entry: http://www.ncbi.nlm.nih.gov/pubmed/21045305 |
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