Abstract

Cerebral cavernous malformation 2 (CCM2) is a novel two-domain adaptor protein which participates in multiple cellular signalling pathways. Loss-of-function mutations in the gene encoding CCM2 are the cause of common human vascular lesions called cerebral cavernous malformations. Here, the purification, crystallization and preliminary X-ray crystallographic studies of the C-terminal domain of CCM2 (CCM2-Ct) are reported. Diffraction data were collected from native and selenomethionine-substituted crystals of CCM2-Ct to resolutions of 2.9 and 2.7 Å, respectively. Both crystals belonged to space group I4(1)22 with similar unit-cell parameters. The native crystals had unit-cell parameters a = b = 113.29, c = 101.62 Å.

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