Production and crystallization of alpha-phosphoglucomutase from Lactococcus lactis

Margarida Archer Frazao; Ana Rute Neves

doi:10.1107/S1744309112032629

Production and crystallization of alpha-phosphoglucomutase from Lactococcus lactis

Margarida Archer Frazao, Ana Rute Neves

Instituto de Tecnologia Química e Biológica António Xavier (ITQB)

Research output: Contribution to journal › Article

2 Citations (Scopus)

Abstract

alpha-Phosphoglucomutase (alpha-PGM) is an enzyme that is essential for the growth of Lactococcus lactis. The enzyme links bacterial anabolism with sugar utilization through glycolysis by catalyzing the reversible interconversion of glucose 6-phosphate and alpha-glucose 1-phosphate. The gene encoding alpha-PGM was cloned and overexpressed in L. lactis. The purified protein was functionally active and was crystallized with ammonium sulfate as a precipitant using vapour-diffusion and seeding techniques. Optimized crystals diffracted to 1.5 angstrom resolution at a synchrotron source.

Original language	Unknown
Pages (from-to)	1113-1115
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	68
Issue number	NA
DOIs	https://doi.org/10.1107/S1744309112032629
Publication status	Published - 1 Jan 2012

Access to Document

10.1107/S1744309112032629

Cite this

@article{58b90229a82c4ad29db8c43cd6cf9e0e,

title = "Production and crystallization of alpha-phosphoglucomutase from Lactococcus lactis",

abstract = "alpha-Phosphoglucomutase (alpha-PGM) is an enzyme that is essential for the growth of Lactococcus lactis. The enzyme links bacterial anabolism with sugar utilization through glycolysis by catalyzing the reversible interconversion of glucose 6-phosphate and alpha-glucose 1-phosphate. The gene encoding alpha-PGM was cloned and overexpressed in L. lactis. The purified protein was functionally active and was crystallized with ammonium sulfate as a precipitant using vapour-diffusion and seeding techniques. Optimized crystals diffracted to 1.5 angstrom resolution at a synchrotron source.",

keywords = "Lactococcus lactis, a-phosphoglucomutase",

author = "Frazao, {Margarida Archer} and Neves, {Ana Rute}",

year = "2012",

month = jan,

day = "1",

doi = "10.1107/S1744309112032629",

language = "Unknown",

volume = "68",

pages = "1113--1115",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

issn = "1744-3091",

publisher = "International Union of Crystallography",

number = "NA",

}

TY - JOUR

T1 - Production and crystallization of alpha-phosphoglucomutase from Lactococcus lactis

AU - Frazao, Margarida Archer

AU - Neves, Ana Rute

PY - 2012/1/1

Y1 - 2012/1/1

N2 - alpha-Phosphoglucomutase (alpha-PGM) is an enzyme that is essential for the growth of Lactococcus lactis. The enzyme links bacterial anabolism with sugar utilization through glycolysis by catalyzing the reversible interconversion of glucose 6-phosphate and alpha-glucose 1-phosphate. The gene encoding alpha-PGM was cloned and overexpressed in L. lactis. The purified protein was functionally active and was crystallized with ammonium sulfate as a precipitant using vapour-diffusion and seeding techniques. Optimized crystals diffracted to 1.5 angstrom resolution at a synchrotron source.

AB - alpha-Phosphoglucomutase (alpha-PGM) is an enzyme that is essential for the growth of Lactococcus lactis. The enzyme links bacterial anabolism with sugar utilization through glycolysis by catalyzing the reversible interconversion of glucose 6-phosphate and alpha-glucose 1-phosphate. The gene encoding alpha-PGM was cloned and overexpressed in L. lactis. The purified protein was functionally active and was crystallized with ammonium sulfate as a precipitant using vapour-diffusion and seeding techniques. Optimized crystals diffracted to 1.5 angstrom resolution at a synchrotron source.

KW - Lactococcus lactis

KW - a-phosphoglucomutase

U2 - 10.1107/S1744309112032629

DO - 10.1107/S1744309112032629

M3 - Article

VL - 68

SP - 1113

EP - 1115

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

SN - 1744-3091

IS - NA

ER -