ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Crystallization and preliminary X-ray diffraction analysis of biotin acetyl-CoA carboxylase ligase (BirA) from Mycobacterium tuberculosis.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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6 authors at 2 institutions in 1 country.
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Abstract
The gene encoding biotin acetyl-CoA carboxylase ligase (BirA) from Mycobacterium tuberculosis was cloned and expressed in Escherichia coli with a C-terminal Strep-tag. PEG 4000 as well as PEG 8000 were used as precipitants at pH 7.5 to crystallize the protein using the vapour-diffusion technique. X-ray characterization of crystals at room temperature indicated that the crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 79.7, b = 62.8, c = 105.8 A. Assuming the presence of two BirA molecules in the asymmetric unit, the solvent content of the crystals was 44% (V(M) = 2.2 A(3) Da(-1)). When transferred to a cryoprotectant, crystals grown in the same drop exhibited a difference in one unit-cell parameter, with a = 60.1, b = 64.0, c = 103.6 A, but belonged to the same P2(1)2(1)2(1) space group. These crystals, with two molecules of BirA present per asymmetric unit, appeared to have a very low solvent content of 28% (V(M) = 1.7 A(3) Da(-1)).
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