Published September 2015 | Version v1
Journal article

Crystallization and preliminary X-ray diffraction study of phosphopantetheine adenylyltransferase from M. tuberculosis crystallizing in space group P32

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

Description

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. P32 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

Additional details

Identifiers

Publishing Information

Journal Title
Crystallography Reports
Journal Volume
60
Journal Issue
5
Journal Page Range
p. 682-684
ISSN
1063-7745
CODEN
CYSTE3

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Copyright
Copyright (c) 2015 Pleiades Publishing, Inc.