Crystallization and preliminary X-ray diffraction studies of beta-phosphoglucomutase from Lactococcus lactus
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/344628
- author
- Lahiri, SD ; Zhang, GF ; Rådström, Peter LU ; Dunaway-Mariano, D and Allen, KN
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Acta Crystallographica. Section D: Biological Crystallography
- volume
- 58
- pages
- 324 - 326
- publisher
- John Wiley & Sons Inc.
- 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
- 2016-04-01 16:45:07
- date last changed
- 2022-03-22 20:52:23
@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 = {{John Wiley & Sons Inc.}},
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}},
doi = {{10.1107/S0907444901019989}},
volume = {{58}},
year = {{2002}},
}