Crystallization and initial X‐ray analysis of rabbit mature sterol carrier protein 2

Sterol carrier protein 2 (SCP2) is a basic intracellular protein which facilitates the in vitrointermembrane transfer of cholesterol, phospholipids and glycolipids. SCP2 was expressed in Escherichia coli, purified to apparent electrophoretic homogeneity and crystallized. Single crystals were obtained by hanging‐drop vapour diffusion using ammonium sulfate as precipitant. These crystals belong to space group P41212 or its enantiomorph, with unit‐cell parameters a= b= 57.5, c= 86.5 Å, and have one molecule in the crystallographic asymmetric unit. Intensity data to 1.8 Å resolution were collected from native SCP2 crystals using synchrotron radiation, were processed and scaled with an Rlinear= 4.9%.