Open AccessPreliminary crystallographic analysis of glyceraldehyde‐3‐phosphate dehydrogenase 3 from Saccharomyces cerevisiae
Author(s) -
Liu Qiao,
Wang Hong,
Liu Huihui,
Teng Maikun,
Li Xu
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112028989
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , dehydrogenase , saccharomyces cerevisiae , glyceraldehyde , biochemistry , glycolysis , gene isoform , enzyme , yeast , chemistry , biology , crystallography , gene
Glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) is an important enzyme in the glycolytic pathway. In addition to its conventional metabolic role, GAPDH has been identified to possess diverse cellular functions. In this study, glyceraldehyde‐3‐phosphate dehydrogenase 3, the third isoform of GAPDH from Saccharomyces cerevisiae , was cloned, expressed, purified and crystallized. The crystals belonged to space group I 4 1 22, with unit‐cell parameters a = b = 116.13, c = 119.21 Å. X‐ray diffraction data were collected to a resolution of 2.6 Å. The structure was solved by molecular replacement and refinement is in progress.