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Crystallization and preliminary analysis of enzyme-substrate complexes of pyruvate kinase from rabbit muscle

✍ Scribed by Karen Schmidt-Bäse; Jenny L. Buchbinder; George H. Reed; Ivan Rayment

Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
494 KB
Volume
11
Category
Article
ISSN
0887-3585

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✦ Synopsis

Abstract

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.

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