Crystallization and X-ray crystallographic analysis of human STAT1.
Unphosphorylated human STAT1 (1-683) has been crystallized in the presence of a phosphopeptide derived from the alpha-chain of human interferon gamma (IFNgamma) receptor. A complete data set has been collected from a KAu(CN)2-derivatized and dehydrated crystal. The crystal belonged to space group P6(1)22, with unit-cell parameters a = b = 102.6, c = 646.5 A, alpha = beta = 90, gamma = 120 degrees.
Mao
Xiang
X
Department of Biochemistry and Molecular Biology, The University of Texas M. D. Anderson Cancer Center, Box 117, Houston, TX 77030, USA.
Chen
Xiaomin
X
D018360:Crystallography, X-Ray / Q000379:methods*; D019281:Dimerization; D006801:Humans; D007371:Interferon-gamma / Q000378:metabolism; D015233:Models, Statistical; D010455:Peptides / Q000737:chemistry; D010766:Phosphorylation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D050794:STAT1 Transcription Factor / Q000737:chemistry*; D014961:X-Ray Diffraction
D010455:Peptides; D050794:STAT1 Transcription Factor; C494079:STAT1 protein, human; D007371:Interferon-gamma