Purification, crystallization, and preliminary X-ray diffraction study of purine nucleoside phosphorylase from E. coli

Journal Article · Wed Jul 15 00:00:00 EDT 2015 · Crystallography Reports

DOI:https://doi.org/10.1134/S1063774515040021· OSTI ID:22472239

Muravieva, T. I.; Esipov, R. S. ^[1]; Kuranova, I. P. ^[2]

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1. Russian Academy of Sciences, Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry (Russian Federation)
2. Russian Academy of Sciences, Shubnikov Institute of Crystallography (Russian Federation)

Crystals of E. coli purine nucleoside phosphorylase were grown in microgravity by the capillary counter-diffusion method through a gel layer. The X-ray diffraction data set suitable for the determination of the three-dimensional structure at atomic resolution was collected from one crystal at the Spring-8 synchrotron facility to 0.99 Å resolution. The crystals belong to sp. gr. P2{sub 1} and have the following unit-cell parameters: a = 74.1 Å, b = 110.2 Å, c = 88.2 Å, α = γ = 90°, β = 111.08°. The crystal contains six subunits of the enzyme comprising a hexamer per asymmetric unit. The hexamer is the biological active form of E. coli. purine nucleoside phosphorylase.

• OSTI ID: 22472239
• Journal Information: Crystallography Reports, Vol. 60, Issue 4; Other Information: Copyright (c) 2015 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7745
• Country of Publication: United States
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
ASYMMETRY
CAPILLARIES
CRYSTAL STRUCTURE
CRYSTALLIZATION
CRYSTALS
DIFFUSION
ESCHERICHIA COLI
LAYERS
NUCLEOSIDES
PHOSPHOTRANSFERASES
PURIFICATION
RESOLUTION
SPRING-8 STORAGE RING
THREE-DIMENSIONAL LATTICES
X-RAY DIFFRACTION