Crystallization and preliminary X-ray analysis of inorganic polyphosphate/ATP-glucomannokinase from Arthrobacter sp. strain KM.

Inorganic polyphosphate [poly(P)]/ATP-glucomannokinase from Arthrobacter sp. Strain KM phosphorylates glucose and mannose, utilizing both ATP and poly(P) as phosphoryl donors. The enzyme was overexpressed in Escherichia coli, purified and crystallized by means of the hanging-drop vapour-diffusion method with ammonium sulfate as the precipitant. The crystals were3 orthorhombic and belonged to space group P2[SUB1]2[SUB1]2[SUB1], with unit-cell parameters a = 66.2, b = 83.7, c = 103.8Å. Assuming two molecules per asymmetric unit, V[SUBsol] is 0.49. X-ray diffraction data to 2.83Å have been collected from a single crystal. [ABSTRACT FROM AUTHOR]