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Crystallization and preliminary analysis of enzyme‐substrate complexes of pyruvate kinase from rabbit muscle
Author(s) -
SchmidtBäse Karen,
Buchbinder Jenny L.,
Reed George H.,
Rayment Ivan
Publication year - 1991
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340110208
Subject(s) - triclinic crystal system , pyruvate kinase , crystallization , crystallography , oxalate , chemistry , substrate (aquarium) , crystal (programming language) , enzyme , resolution (logic) , crystal structure , biochemistry , inorganic chemistry , biology , ecology , organic chemistry , glycolysis , artificial intelligence , computer science , programming language
Pyruvate kinase from rabbit muscle has been crystallized in a form suitable for high resolution X‐ray analysis. Complexes of the enzyme with Mn 2+ and either pyruvate or oxalate crystallize from solutions of polyethyleneglycol 8000 at pH 6.0. Crystals obtained from solutions of the complexes with pyruvate or oxalate appear isomorphous and belong to the triclinic space group P1. The crystals have unit cell dimensions a = 83.3(4) Å, b = 109.4(6) Å, c = 145.7(7) Å, α = 94.9°, β = 93.6°, γ = 112.2°. These crystals diffract to better than 2.4 Å resolution and are stable in the X‐ray beam for at least 20 hr. Electron paramagnetic resonance measurements on a single crystal show that Mn 2+ is bound to the crystalline protein.