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.

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

MATTEVI, ANDREA;VALENTINI, GIOVANNA;SPERANZA, MARIA LUISA;CODA, ALESSANDRO
1995-01-01

Abstract

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.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11571/137462
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