Publication Date:
2016-05-23
Description:
Thioredoxin is a small ubiquitous protein that plays a role in many biological processes. A putative thioredoxin, Trx1, fromThermosipho africanusstrain 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 MMgCl2, 0.1 Mbis-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 groupP212121, with unit-cell parametersa= 40.6,b= 41.5,c= 56.4 Å, α = β = γ = 90.0°.
Electronic ISSN:
2053-230X
Topics:
Biology
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Chemistry and Pharmacology
,
Geosciences
,
Physics
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