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Title: Crystallization and preliminary X-ray diffraction study of phosphopantetheine adenylyltransferase from M. tuberculosis crystallizing in space group P3{sub 2}

Crystals of M. tuberculosis phosphopantetheine adenylyltransferase 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 2.00-Å resolution. The crystals belong to sp. gr. P3{sub 2} and have the following unit-cell parameters: a = b = 106.47 Å, c = 71.32 Å, α = γ = 90°, β = 120°. The structure was solved by the molecular-replacement method. There are six subunits of the enzyme comprising a hexamer per asymmetric unit. The hexamer is a biologically active form of phosphopantetheine adenylyltransferase from M. tuberculosis.
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:
22472147
Resource Type:
Journal Article
Resource Relation:
Journal Name: Crystallography Reports; Journal Volume: 60; Journal Issue: 5; 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; CAPILLARIES; CRYSTAL GROWTH; CRYSTAL STRUCTURE; CRYSTALLIZATION; CRYSTALS; DIFFUSION; ENZYMES; GELS; LAYERS; SPRING-8 STORAGE RING; THREE-DIMENSIONAL LATTICES; TUBERCULOSIS; X-RAY DIFFRACTION