Open AccessCharacterization, crystallization and preliminary X‐ray investigation of glyceraldehyde‐3‐phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus
Author(s) -
Fleming T. M.,
Jones C. E.,
Piper P. W.,
Cowan D. A.,
Isupov M. N.,
Littlechild J. A.
Publication year - 1998
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444997018076
Subject(s) - sulfolobus solfataricus , dehydrogenase , tetramer , cofactor , ammonium sulfate , glyceraldehyde 3 phosphate dehydrogenase , nad+ kinase , sulfolobus , crystallography , biochemistry , archaea , enzyme , biology , chemistry , chromatography , gene
Recombinant Sulfolobus solfataricus glyceraldehyde‐3‐phosphate dehydrogenase has been purified and found to be a tetramer of 148 kDa. The enzyme shows dual cofactor specificity and uses NADP + in preference to NAD + . The sequence has been compared with other GAPDH proteins including those from other archaeal sources. The purified protein has been crystallized from ammonium sulfate to produce crystals that diffract to 2.4 Å with a space group of P 4 3 2 1 2 or P 4 1 2 1 2. A native data set has been collected to 2.4 Å using synchrotron radiation and cryocooling.
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