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Crystallization and preliminary X-ray diffraction studies of beta-phosphoglucomutase from Lactococcus lactus

Lahiri, SD; Zhang, GF; Rådström, Peter LU ; Dunaway-Mariano, D and Allen, KN (2002) In Acta Crystallographica. Section D: Biological Crystallography 58. p.324-326
Abstract
beta-Phosphoglucomutase (beta-PGM), a 28 kDa monomer, catalyzes the reversible conversion of beta-D-glucose-1-phosphate to beta-D-glucose-6-phosphate in maltose metabolism in a variety of organisms. Sequence analysis of beta-PGM indicates that it is a member of the haloacid dehalogenase (HAD) enzyme superfamily, which evolved to cleave C-Cl, C-P and C-OP bonds in a variety of substrates. beta-PGM has been crystallized using the hanging-drop method. Diffraction-quality crystals of the native protein have been obtained from two conditions, both belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.67, b = 92.78, c = 111.60 and a = 53.21, b = 57.01, c = 76.11 Angstrom. To solve the phase problem, selenomethionine (SeMet)... (More)
beta-Phosphoglucomutase (beta-PGM), a 28 kDa monomer, catalyzes the reversible conversion of beta-D-glucose-1-phosphate to beta-D-glucose-6-phosphate in maltose metabolism in a variety of organisms. Sequence analysis of beta-PGM indicates that it is a member of the haloacid dehalogenase (HAD) enzyme superfamily, which evolved to cleave C-Cl, C-P and C-OP bonds in a variety of substrates. beta-PGM has been crystallized using the hanging-drop method. Diffraction-quality crystals of the native protein have been obtained from two conditions, both belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.67, b = 92.78, c = 111.60 and a = 53.21, b = 57.01, c = 76.11 Angstrom. To solve the phase problem, selenomethionine (SeMet) containing alpha-PGM crystals have been grown. The SeMet-containing crystals diffract to high resolution only when grown by microseeding with native crystals. A three-wavelength data set has been collected to 2.3 Angstrom on crystals of the SeMet-substituted beta-PGM. The structure solution is currently being attempted by the multi-wavelength anomalous diffraction (MAD) phasing method. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Acta Crystallographica. Section D: Biological Crystallography
volume
58
pages
324 - 326
publisher
International Union of Crystallography
external identifiers
  • pmid:11807265
  • wos:000173442200023
  • scopus:0036008540
ISSN
1399-0047
DOI
10.1107/S0907444901019989
language
English
LU publication?
yes
id
1dad6397-975a-4f12-9b61-2fc91dec816c (old id 344628)
date added to LUP
2007-11-05 15:20:14
date last changed
2017-12-10 04:36:16
@article{1dad6397-975a-4f12-9b61-2fc91dec816c,
  abstract     = {beta-Phosphoglucomutase (beta-PGM), a 28 kDa monomer, catalyzes the reversible conversion of beta-D-glucose-1-phosphate to beta-D-glucose-6-phosphate in maltose metabolism in a variety of organisms. Sequence analysis of beta-PGM indicates that it is a member of the haloacid dehalogenase (HAD) enzyme superfamily, which evolved to cleave C-Cl, C-P and C-OP bonds in a variety of substrates. beta-PGM has been crystallized using the hanging-drop method. Diffraction-quality crystals of the native protein have been obtained from two conditions, both belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.67, b = 92.78, c = 111.60 and a = 53.21, b = 57.01, c = 76.11 Angstrom. To solve the phase problem, selenomethionine (SeMet) containing alpha-PGM crystals have been grown. The SeMet-containing crystals diffract to high resolution only when grown by microseeding with native crystals. A three-wavelength data set has been collected to 2.3 Angstrom on crystals of the SeMet-substituted beta-PGM. The structure solution is currently being attempted by the multi-wavelength anomalous diffraction (MAD) phasing method.},
  author       = {Lahiri, SD and Zhang, GF and Rådström, Peter and Dunaway-Mariano, D and Allen, KN},
  issn         = {1399-0047},
  language     = {eng},
  pages        = {324--326},
  publisher    = {International Union of Crystallography},
  series       = {Acta Crystallographica. Section D: Biological Crystallography},
  title        = {Crystallization and preliminary X-ray diffraction studies of beta-phosphoglucomutase from Lactococcus lactus},
  url          = {http://dx.doi.org/10.1107/S0907444901019989},
  volume       = {58},
  year         = {2002},
}