ArticleActa crystallographica. Section F, Structural biology communications2016
Putative thioredoxin Trx1 from Thermosipho africanus strain TCF52B: expression, purification and structural determination using S-SAD.
Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Thioredoxin is a small ubiquitous protein that plays a role in many biological processes. A putative thioredoxin, Trx1, from Thermosipho africanus strain TCF52B, which has low sequence identity to its closest homologues, was successfully cloned, overexpressed and purified. The protein was crystallized using the microbatch-under-oil technique at 289 K in a variety of conditions; crystals grown in 0.2 M MgCl2, 0.1 M bis-tris pH 6.5, 25%(w/v) PEG 3350, which grew as irregular trapezoids to maximum dimensions of 1.2 × 1.5 × 0.80 mm, were used for sulfur single-wavelength anomalous dispersion analysis. The anomalous sulfur signal could be detected to 2.83 Å resolution using synchrotron radiation on the 08B1-1 beamline at the Canadian Light Source. The crystals belonged to space group P212121, with unit-cell parameters a = 40.6, b = 41.5, c = 56.4 Å, α = β = γ = 90.0°.
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