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Crystallization and initial X-ray diffraction analysis of the tellurite-resistance S-adenosyl-L-methionine transferase protein TehB from Escherichia coli.

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, ? = 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, ? = 95.9°.

SUBMITTER: Choudhury HG

PROVIDER: S-EPMC3001658 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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Crystallization and initial X-ray diffraction analysis of the tellurite-resistance S-adenosyl-L-methionine transferase protein TehB from Escherichia coli.

Choudhury Hassanul Ghani HG Beis Konstantinos K

Acta crystallographica. Section F, Structural biology and crystallization communications 20101028 Pt 11

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 par ...[more]

PMID: 21045305

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