Crystallization and preliminary X-ray diffraction study of recombinant ribokinase from Thermus Species 2.9

Abstract

Ribokinase from a thermophilic strain of Thermus species 2.9 belonging to the carbohydrate ribokinase family (EC 2.7.1.15) was isolated, purified, and crystallized. The crystallization conditions were found by the vapor-diffusion technique and were then optimized to apply the capillary counter-diffusion technique. The X-ray diffraction data set was collected from the crystals, which were grown by the counter-diffusion technique, at the SPring-8 synchrotron radiation facility to 2.87 A resolution. The crystals belong to sp. gr. P1211 and have the following unit-cell parameters: a = 81.613 A, b = 156.132 A, c = 87.714 A, α = γ = 90°, β = 103.819°. The X-ray diffraction data set is suitable for determining the three-dimensional structure of the protein by the molecular-replacement method.