Expression, purification and preliminary crystallographic analysis of recombinant human small glutamine-rich tetratricopeptide-repeat protein.
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 A. Crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 67.82, b = 81.93, c = 55.92 A, alpha = beta = gamma = 90 degrees .
Dutta
Sujit
S
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.
Kotaka
Masayo
M
Tan
Yee Joo
YJ
D002352:Carrier Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification; D018360:Crystallography, X-Ray; D006801:Humans; D018832:Molecular Chaperones; D017434:Protein Structure, Tertiary / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D020449:Repetitive Sequences, Amino Acid / Q000235:genetics; D020080:Tandem Repeat Sequences / Q000235:genetics; D054334:Viral Regulatory and Accessory Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification
D002352:Carrier Proteins; D018832:Molecular Chaperones; D011994:Recombinant Proteins; C114575:SGTA protein, human; D054334:Viral Regulatory and Accessory Proteins