Lactate dehydrogenase from the hyperthermophilic archaeon Methanococcus jannaschii: overexpression, crystallization and preliminary X-ray analysis.

@article{Lee2000LactateDF,
  title={Lactate dehydrogenase from the hyperthermophilic archaeon Methanococcus jannaschii: overexpression, crystallization and preliminary X-ray analysis.},
  author={Byung Il Lee and Changsoo Chang and Su Jin Cho and Gye Won Han and Yeon Gyu Yu and Soo Hyun Eom and Se Won Suh},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2000},
  volume={56 Pt 1},
  pages={81-3}
}
L(+)-Lactate dehydrogenase (LDH) is a key enzyme in anaerobic metabolism which converts pyruvate to lactate. LDH from the hyperthermophilic archaebacterium Methanococcus jannaschii has been overexpressed in Escherichia coli and crystallized in two crystal forms at 297 K using 2-methyl-2,4-pentanediol as precipitant. Type I crystals grew rapidly and… CONTINUE READING