Expression, purification and preliminary crystallographic analysis of recombinant human small glutamine-rich tetratricopeptide-repeat protein
- Cancer and Developmental Cell Biology Division, Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), 61 Biopolis Drive, Singapore 138673 (Singapore)
- School of Biological Sciences, Nanyang Technological University, Singapore 637551 (Singapore)
The production and crystallization of the tetratricopeptide-repeat domain of human small glutamine-rich tetratricopeptide-repeat protein are reported. A 2.4 Å native diffraction data set has been obtained. Human small glutamine-rich tetratricopeptide-repeat protein (hSGT) is a 35 kDa protein implicated in a number of biological processes that include apoptosis, cell division and intracellular cell transport. The tetratricopeptide-repeat (TPR) domain of hSGT has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of the TPR domain of hSGT is reported. X-ray diffraction data were processed to a resolution of 2.4 Å. Crystals belong to space group P2{sub 1}2{sub 1}2, with unit-cell parameters a = 67.82, b = 81.93, c = 55.92 Å, α = β = γ = 90°.
- OSTI ID:
- 22360592
- Journal Information:
- Acta Crystallographica. Section F, Vol. 64, Issue Pt 7; Other Information: PMCID: PMC2443970; PMID: 18607086; PUBLISHER-ID: hc5051; OAI: oai:pubmedcentral.nih.gov:2443970; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Crystal Structures of the Tetratricopeptide Repeat Domains of Kinesin Light Chains: Insight into Cargo Recognition Mechanisms
Expression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14–16