Open AccessExpression, purification and preliminary crystallographic analysis of recombinant human small glutamine‐rich tetratricopeptide‐repeat protein
Author(s) -
Dutta Sujit,
Kotaka Masayo,
Tan YeeJoo
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108009299
Subject(s) - tetratricopeptide , recombinant dna , escherichia coli , crystallization , intracellular , resolution (logic) , glutamine , chemistry , nucleoid , biology , crystallography , microbiology and biotechnology , biochemistry , gene , amino acid , organic chemistry , artificial intelligence , computer science
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 P 2 1 2 1 2, with unit‐cell parameters a = 67.82, b = 81.93, c = 55.92 Å, α = β = γ = 90°.