Crystallization and preliminary crystallographic analysis of the ezrin FERM domain

20 July 2002

journal article
research article
Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography

Vol. 58 (8) , 1359-1361
https://doi.org/10.1107/s0907444902010004

Abstract

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.

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