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Expression, purification, crystallization and preliminary crystallographic study of the cytoplasmic domain of the mitochondrial dynamics protein MiD51
Author(s) -
Ma Jun,
Sun Fei
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14006827
Subject(s) - mitochondrial fission , organelle , mitochondrion , cytoplasm , crystallization , fission , mitochondrial fusion , biophysics , crystallography , chemistry , microbiology and biotechnology , biology , biochemistry , physics , mitochondrial dna , nuclear physics , gene , organic chemistry , neutron
Mitochondria play central roles in many cellular and physiological processes. They are highly dynamic organelles and continually undergo fusion and fission. Mitochondrial dynamics protein 51 kDa (MiD51), an integral mitochondrial outer membrane protein, recruits dynamin‐related protein 1 (Drp1; a mitochondrial fission protein) to mitochondria and facilitates Drp1‐directed mitochondrial fission. In this study, the cytoplasmic domain of MiD51 was overexpressed in Escherichia coli , purified and crystallized. An X‐ray diffraction data set was collected to a resolution of 3.1 Å and the crystal belonged to space group P 4 1 2 1 2, with unit‐cell parameters a = b = 90.1, c = 124.7 Å, α = β = γ = 90°. The asymmetric unit had the highest probability of containing one molecule, with a Matthews coefficient of 3.32 Å 3 Da −1 and a solvent content of 63.0%.