Open AccessCrystallization and preliminary X‐ray analysis of the C‐terminal domain of CCM2, part of a novel adaptor protein involved in cerebral cavernous malformations
Author(s) -
Wang Xiaoyan,
Ding Jingjin,
Wang Dacheng
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112016181
Subject(s) - signal transducing adaptor protein , crystallography , crystallization , x ray , domain (mathematical analysis) , chemistry , gene , biology , biophysics , biochemistry , physics , optics , mathematical analysis , mathematics , organic chemistry
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 I 4 1 22 with similar unit‐cell parameters. The native crystals had unit‐cell parameters a = b = 113.29, c = 101.62 Å.