Abstract
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 .
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Carrier Proteins / biosynthesis*
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Carrier Proteins / genetics
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Carrier Proteins / isolation & purification
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Crystallography, X-Ray
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Humans
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Molecular Chaperones
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Protein Structure, Tertiary / genetics
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / genetics*
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Recombinant Proteins / isolation & purification
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Repetitive Sequences, Amino Acid / genetics
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Tandem Repeat Sequences / genetics
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Viral Regulatory and Accessory Proteins / biosynthesis
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Viral Regulatory and Accessory Proteins / genetics*
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Viral Regulatory and Accessory Proteins / isolation & purification
Substances
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Carrier Proteins
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Molecular Chaperones
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Recombinant Proteins
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SGTA protein, human
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Viral Regulatory and Accessory Proteins