Crystallization and preliminary X-ray crystallographic analysis of rat calcineurin B homologous protein 1

Abstract

Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding protein that plays a role in membrane trafficking and binds to multiple effector proteins, including Na+/H+ exchangers, serine/threonine protein kinase and calcineurin, potentially modulating their function. CHP1 has been crystallized at 277 K using polyethylene glycol as a precipitant. The crystal belongs to space group P2(1), with unit-cell parameters a = 55.5, b = 38.5, c = 90.0 A, beta = 90.7 degrees. A full set of diffraction data was collected to 2.2 A resolution at 100 K using the Photon Factory synchrotron-radiation source.