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Phosphoglycerate kinase from the extreme thermophile Thermus thermophilus Crystallization and preliminary X‐ray data
Author(s) -
Littlechild J.A.,
Davies G.J.,
Gamblin S.J.,
Watson H.C.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81143-2
Subject(s) - thermus thermophilus , thermophile , phosphoglycerate kinase , thermus , crystallization , pyruvate kinase , crystallography , enzyme , biology , chemistry , biochemistry , glycolysis , escherichia coli , organic chemistry , gene
The glycolytic enzyme phosphoglycerate kinase has been prepared from the extreme thermophile Thermus thermophilus . In contrast to its eukaryote equivalents (yeast and horse muscle) this prokaryotic enzyme crystallizes from ammonium sulphate in the presence of nucleotide substrates. These crystals are of a form and size well suited to high resolution X‐ray diffraction study using rotation camera techniques.