Crystallization and preliminary crystallographic analysis of the ezrin FERM domain.
Ezrin is a member of the ERM (ezrin/radixin/moesin) family of proteins that cross-link the actin cytoskeleton to the plasma membrane and that also function, both upstream and downstream of the small G-protein Rho, in signaling cascades that regulate the assembly of actin stress fibers. In this study, crystals were obtained of the amino-terminal 297 residues (referred to as FERM) of ezrin. The crystals of the FERM domain of ezrin belong to the monoclinic space group P2(1), with unit-cell parameters a = 48.5, b = 112.8, c = 66.3 A, beta = 102.3 degrees, and contain two molecules in the asymmetric unit. A 2.3 A data set was collected using synchrotron radiation at CHESS A1.
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
William J
WJ
Smith
Richard A
RA
Cerione
D003460:Crystallization; D018360:Crystallography, X-Ray; D003598:Cytoskeletal Proteins; D006801:Humans; D010750:Phosphoproteins / Q000737:chemistry* / Q000302:isolation & purification; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D000099149:Ezrin
D003598:Cytoskeletal Proteins; D010750:Phosphoproteins; D011994:Recombinant Proteins; D000099149:Ezrin