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Clostridium beijerinckii glyceraldehyde-3-phosphate dehydrogenase GAPDH: purification, crystallization, and X-ray crystallographic analysis
Clostridium beijerinckii glyceraldehyde-3-phosphate dehydrogenase GAPDH: purification, crystallization, and X-ray crystallographic analysis
- 한국구조생물학회
- Biodesign
- Vol 10, No 3, Sep
- : KCI등재후보
- 2022.09
- 51 - 55 (5 pages)
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous and highly abundant glycolytic enzyme. It plays a pivotal role for the energy and carbon metabolism of most organisms including industrial bacteria. It catalyzes the two step oxidative phosphorylation of D-glyceraldehyde-3-phosphate into 1,3-bisphosphoglycerate using inorganic phosphate and nicotinamide adenine dinucleotide (NAD+) as cofactor. In this study, GAPDH from C. beijerinckii (CbGAPDH) was successfully expressed and purified using Ni-NTA affinity, Q anion-exchange, and gel-filtration chromatography. The protein crystal was obtained and diffracted to a resolution of 1.60 Å. The crystal belonged to the hexagonal space group P6222, with unit-cell parameters of a = 120.6, b = 120.6, and c = 122.1 Å. The Matthews coefficient and solvent content were estimated to be 3.50 Å3 Da–1 and 64.90%, respectively, assuming that the asymmetric unit contained only one recombinant protein molecule.