Expression, purification, crystallization and preliminary X-ray diffraction analysis of thioredoxin Trx1 from Saccharomyces cerevisiae

Journal Article · Tue Apr 01 04:00:00 EDT 2008 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309108004612· OSTI ID:22360512

Zhang, Yaru; Bao, Rui ^[1]; Zhou, Cong-Zhao ^[2]; Chen, Yuxing ^[1]

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1. Institute of Protein Research, Tongji University, Shanghai 200092 (China)
2. Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026 (China)

In the present work, the cytosolic form of thioredoxin from S. cerevisiae was cloned, expressed, purified and crystallized. Thioredoxins play key roles in the cellular response to oxidative stress. Three isoforms of thioredoxin have been identified in Saccharomyces cerevisiae: two that are cytosolic (Trx1 and Trx2) and one that is mitochondrial (Trx3). In the present work, the cytosolic form Trx1 was cloned, expressed, purified and crystallized. Crystals were obtained by the hanging-drop vapour-diffusion method. A data set was collected from a single crystal to 1.7 Å resolution. The crystal belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 32.29, b = 46.59, c = 64.20 Å, α = β = γ = 90°.

• OSTI ID: 22360512
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 4 Vol. 64; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
DIFFUSION
MONOCRYSTALS
RESOLUTION
SPACE GROUPS
X-RAY DIFFRACTION