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Updated: May 20, 2026

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
Published on: March 20, 2021
Crystallization and preliminary crystallographic studies of CCM3 in complex with the C-terminal domain of MST4
Xueyong Xu1, Xiaoyan Wang, Jingjin Ding
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Abstract:
MST4 is a member of the GCKIII kinases. The interaction between cerebral cavernous malformation 3 (CCM3) and GCKIII kinases plays a critical role in cardiovascular development and in cerebral cavernous malformations. The complex of CCM3 and the C-terminal domain of MST4 has been constructed, purified and crystallized, and a diffraction data set has been collected to 2.4 Å resolution. The crystal of the CCM3-MST4 C-terminal domain complex belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = 69.10, b = 69.10, c = 117.57 Å.
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