Schmidt-Bäse K, Buchbinder J L, Reed G H, Rayment I
Institute for Enzyme Research, University of Wisconsin, Madison 53705.
Proteins. 1991;11(2):153-7. doi: 10.1002/prot.340110208.
Pyruvate kinase from rabbit muscle has been crystallized in a form suitable for high resolution X-ray analysis. Complexes of the enzyme with Mn2+ and either pyruvate or oxalate crystallize from solutions of polyethyl-eneglycol 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) A, b = 109.4(6) A, c = 145.7 (7) A, alpha = 94.9 degrees, beta = 93.6 degrees, gamma = 112.2 degrees. These crystals diffract to better than 2.4 A resolution and are stable in the X-ray beam for at least 20 hr. Electron paramagnetic resonance measurements on a single crystal show that Mn2+ is bound to the crystalline protein.
来自兔肌肉的丙酮酸激酶已结晶成适合高分辨率X射线分析的形式。该酶与Mn2+以及丙酮酸或草酸盐的复合物在pH 6.0的聚乙二醇8000溶液中结晶。从与丙酮酸或草酸盐的复合物溶液中获得的晶体呈现同晶型，属于三斜晶系空间群P1。晶体的晶胞参数为a = 83.3(4) Å，b = 109.4(6) Å，c = 145.7 (7) Å，α = 94.9度，β = 93.6度，γ = 112.2度。这些晶体的衍射分辨率优于2.4 Å，并且在X射线束中至少稳定20小时。对单晶进行的电子顺磁共振测量表明，Mn2+与结晶蛋白结合。
