Crystallization and preliminary crystallographic analysis of the fourth FAS1 domain of human BigH3.
The protein BigH3 is a cell-adhesion molecule induced by transforming growth factor-beta (TGF-beta). It consists of four homologous repeat domains known as FAS1 domains; mutations in these domains have been linked to corneal dystrophy. The fourth FAS1 domain was expressed in Escherichia coli B834 (DE3) (a methionine auxotroph) and purified by DEAE anion-exchange and gel-filtration chromatography. The FAS1 domain was crystallized using the vapour-diffusion method. A SAD diffraction data set was collected to a resolution of 2.5 A at 100 K. The crystal belonged to space group P6(1) or P6(5) and had two molecules per asymmetric unit, with unit-cell parameters a = b = 62.93, c = 143.27 A, alpha = beta = 90.0, gamma = 120.0 degrees.
Yoo
Ji-Ho
JH
Department of Biology, Yonsei University, South Korea.
Kim
EungKweon
E
Kim
Jongsun
J
Cho
Hyun-Soo
HS
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004331:Drosophila melanogaster; D016326:Extracellular Matrix Proteins / Q000737:chemistry / Q000302:isolation & purification*; D006801:Humans; D016212:Transforming Growth Factor beta / Q000737:chemistry / Q000302:isolation & purification*; D019014:fas Receptor / Q000737:chemistry / Q000302:isolation & purification*; D000099222:betaIG-H3 Protein
D016326:Extracellular Matrix Proteins; D016212:Transforming Growth Factor beta; D019014:fas Receptor; D000099222:betaIG-H3 Protein; C491901:FAS protein, human