NDUFA2 is a supernumerary subunit of the mitochondrial respiratory complex I and is implicated in Leigh’s disease and leukoencephalopathy. We overexpressed human NDUFA2 in E. coli and purified the protein by the His-tag affinity chromatography and size-exclusion chromatography. The NDUFA2 protein was crystallized using the sitting drop vapordiffusion method with the mother liquor of 50 mM CAPS pH 10.5 and PEG3350 15% at 18°C. The crystals diffracted to 2.43 Å resolution. The NDUFA2 crystals belonged to the space group P1 with unit cell parameters a = 44.71 Å, b = 70.41 Å, c = 71.05 Å, α = 62.26°, β = 86.06°, and γ = 85.83°. The asymmetric unit of the NDUFA2 crystals contained eight NDUFA2 molecules with a solvent content of 48.4% and a Mathews coefficient of 2.38 Å3/Da. The molecular replacement solution of the crystals resulted in a good-quality of electron density map.
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