ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Crystallization and initial X-ray diffraction analysis of the tellurite-resistance S-adenosyl-L-methionine transferase protein TehB from Escherichia coli.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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2 citing papers in PubMed, 5 citations in OpenAlex.
- Use of Microbial Consortia in Bioremediation of Metalloid Polluted Environments.Microorganisms · 2023Review
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2 authors at 2 institutions in 1 country.
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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°.
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