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Updated: Jun 26, 2026

High Precision FRET at Single-molecule Level for Biomolecule Structure Determination
Published on: May 13, 2017
Purification, crystallization and preliminary X-ray diffraction analysis of glutathionylated Trx1 C33S mutant from
Xiaochu Lou1, Yaru Zhang, Rui Bao
1Institute of Protein Research, Tongji University, Shanghai, People's Republic of China.
Abstract:
Thioredoxins (Trxs) are a family of small redox-active proteins that are found in all living organisms. In Saccharomyces cerevisiae, two cytosolic Trxs (Trx1 and Trx2) and one mitochondrial Trx (Trx3) have previously been identified. In this work, cytosolic Trx1 containing a C33S mutant was overexpressed, purified, glutathionylated and crystallized using the hanging-drop vapour-diffusion method. A set of X-ray diffraction data was collected to 1.80 A resolution. The crystal belonged to space group P1, with unit-cell parameters a = 38.53, b = 38.81, c = 41.70 A, alpha = 72.91, beta = 87.51, gamma = 60.58 degrees.
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