Cryst. Rep, 2018, 63(5):761-764

Crystallization and Preliminary X-ray Diffraction Study of Purine Nucleoside Phosphorylase from the Thermophilic Bacterium Thermus thermophilus Strain HB27

Recombinant purine nucleoside phosphorylase from the thermophilic Thermus thermophilus strain encoded by the TT_C0194 gene was purified to homogeneity. The crystallization conditions for the enzyme were found by the vapor-diffusion technique. The crystals of the enzyme suitable for X-ray diffraction were grown under microgravity conditions by the capillary counter-diffusion method. The crystals belong to sp. gr. P212121and have the following unit-cell parameters: a = 89.9 Å, b = 121.0 Å, c = 215.7 Å, α = β = γ = 90°. The X-ray diffraction data set suitable for the determination of the three-dimensional structure of purine nucleoside phosphorylase was collected from the grown crystals at the SPring-8 synchrotron facility to 2.5 Å resolution.

Sinitsyna EV, Timofeev VI, Zhukhlistova NE, Muravieva TI, Kostromina MA, Esipov RS, Kuranova IP

IBCH: 6622
Ссылка на статью в журнале: http://link.springer.com/10.1134/S1063774518050279
Кол-во цитирований на 03.2024: 1
Данные статьи проверены модераторами 2018-09-27

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