Crystallization and Preliminary X-ray Diffraction Study of Purine Nucleoside Phosphorylase from the Thermophilic Bacterium Thermus thermophilus Strain HB27
- Russian Academy of Sciences, Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry (Russian Federation)
- Russian Academy of Sciences, Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics,” (Russian Federation)
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. P2{sub 1}2{sub 1}2{sub 1} and 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.
- OSTI ID:
- 22758201
- Journal Information:
- Crystallography Reports, Journal Name: Crystallography Reports Journal Issue: 5 Vol. 63; ISSN 1063-7745; ISSN CYSTE3
- Country of Publication:
- United States
- Language:
- English
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