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

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.
Authors:
; ;  [1] ; ;  [2] ;  [1]
  1. Russian Academy of Sciences, Shubnikov Institute of Crystallography (Russian Federation)
  2. Russian Academy of Sciences, Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry (Russian Federation)
Publication Date:
OSTI Identifier:
22472239
Resource Type:
Journal Article
Resource Relation:
Journal Name: Crystallography Reports; Journal Volume: 60; Journal Issue: 4; Other Information: Copyright (c) 2015 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
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