Crystallization and preliminary X-ray analysis of pyruvate kinase type I from Escherichia coli

Autor: Andrea Mattevi, M L Speranza, Martino Bolognesi, P. Sartori, Alessandro Coda, Giovanna Valentini
Rok vydání: 1995
Předmět:
Zdroj: Acta crystallographica. Section D, Biological crystallography. 51(Pt 6)
ISSN: 0907-4449
Popis: Crystals of the fructose-l,6-bisphosphate-dependent pyruvate kinase from Escherichia coli have been grown using the hanging-drop vapour-diffusion technique. The space group was found to be C222(1) with cell dimensions a = 76.8, b = 247.5, c = 132.6 A. Diffraction data to 3.0 A resolution have been recorded and the enzyme molecular symmetry analysed through inspection of the self-rotation function. The crystallized protein is in the allosterically inactive T state.
Databáze: OpenAIRE