PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF PENICILLIN-BINDING PROTEIN-4 FROM ESCHERICHIA-COLI, A PROTEIN RELATED TO CLASS-A BETA-LACTAMASES

MMGM THUNNISSEN; F FUSETTI; B DEBOER; BW DIJKSTRA

PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF PENICILLIN-BINDING PROTEIN-4 FROM ESCHERICHIA-COLI, A PROTEIN RELATED TO CLASS-A BETA-LACTAMASES

MMGM THUNNISSEN^*, F FUSETTI, B DEBOER, BW DIJKSTRA

^*Corresponding author for this work

Research output: Contribution to journal › Comment/Letter to the editor › Academic › peer-review

Abstract

Crystals of the penicillin binding protein 4 (PBP4) from Escherichia coli have been obtained at 37 degrees C from liquid to liquid diffusion experiments in capillaries. PBP4 was dissolved in a 1.0 M ammonium sulphate solution, buffered at pH 7.2, to a concentration of 5 mg/ml, and was layered on top of a 1.6 to 2.2 M ammonium sulphate solution. Crystals appeared within four to six weeks. They belong to space group C222 with cell dimensions a = 68.5 Angstrom, b = 100.5 Angstrom and c = 137.0 Angstrom, and diffract to at least 2.8 Angstrom resolution. There is one molecule with a molecule mass of 49,568 Da in the asymmetric unit.

Original language	English
Pages (from-to)	149-153
Number of pages	5
Journal	Journal of Molecular Biology
Volume	247
Issue number	2
Publication status	Published - 24-Mar-1995

Keywords

CRYSTALLIZATION
PENICILLIN
BINDING PROTEIN
BETA-LACTAMASE
MUREIN
PEPTIDOGLYCAN
REFINED CRYSTAL-STRUCTURE
BACILLUS-LICHENIFORMIS
NUCLEOTIDE-SEQUENCE
NM RESOLUTION
CRYSTALLIZATION
ENZYME
GENE
BIOSYNTHESIS
INHIBITION
RESISTANCE

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@article{a53b34b25622447bbb963465dcdfc0b2,

title = "PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF PENICILLIN-BINDING PROTEIN-4 FROM ESCHERICHIA-COLI, A PROTEIN RELATED TO CLASS-A BETA-LACTAMASES",

abstract = "Crystals of the penicillin binding protein 4 (PBP4) from Escherichia coli have been obtained at 37 degrees C from liquid to liquid diffusion experiments in capillaries. PBP4 was dissolved in a 1.0 M ammonium sulphate solution, buffered at pH 7.2, to a concentration of 5 mg/ml, and was layered on top of a 1.6 to 2.2 M ammonium sulphate solution. Crystals appeared within four to six weeks. They belong to space group C222 with cell dimensions a = 68.5 Angstrom, b = 100.5 Angstrom and c = 137.0 Angstrom, and diffract to at least 2.8 Angstrom resolution. There is one molecule with a molecule mass of 49,568 Da in the asymmetric unit.",

keywords = "CRYSTALLIZATION, PENICILLIN, BINDING PROTEIN, BETA-LACTAMASE, MUREIN, PEPTIDOGLYCAN, REFINED CRYSTAL-STRUCTURE, BACILLUS-LICHENIFORMIS, NUCLEOTIDE-SEQUENCE, NM RESOLUTION, CRYSTALLIZATION, ENZYME, GENE, BIOSYNTHESIS, INHIBITION, RESISTANCE",

author = "MMGM THUNNISSEN and F FUSETTI and B DEBOER and BW DIJKSTRA",

year = "1995",

month = mar,

day = "24",

language = "English",

volume = "247",

pages = "149--153",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "2",

}

PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF PENICILLIN-BINDING PROTEIN-4 FROM ESCHERICHIA-COLI, A PROTEIN RELATED TO CLASS-A BETA-LACTAMASES. / THUNNISSEN, MMGM; FUSETTI, F; DEBOER, B et al.
In: Journal of Molecular Biology, Vol. 247, No. 2, 24.03.1995, p. 149-153.

Research output: Contribution to journal › Comment/Letter to the editor › Academic › peer-review

TY - JOUR

T1 - PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF PENICILLIN-BINDING PROTEIN-4 FROM ESCHERICHIA-COLI, A PROTEIN RELATED TO CLASS-A BETA-LACTAMASES

AU - THUNNISSEN, MMGM

AU - FUSETTI, F

AU - DEBOER, B

AU - DIJKSTRA, BW

PY - 1995/3/24

Y1 - 1995/3/24

N2 - Crystals of the penicillin binding protein 4 (PBP4) from Escherichia coli have been obtained at 37 degrees C from liquid to liquid diffusion experiments in capillaries. PBP4 was dissolved in a 1.0 M ammonium sulphate solution, buffered at pH 7.2, to a concentration of 5 mg/ml, and was layered on top of a 1.6 to 2.2 M ammonium sulphate solution. Crystals appeared within four to six weeks. They belong to space group C222 with cell dimensions a = 68.5 Angstrom, b = 100.5 Angstrom and c = 137.0 Angstrom, and diffract to at least 2.8 Angstrom resolution. There is one molecule with a molecule mass of 49,568 Da in the asymmetric unit.

AB - Crystals of the penicillin binding protein 4 (PBP4) from Escherichia coli have been obtained at 37 degrees C from liquid to liquid diffusion experiments in capillaries. PBP4 was dissolved in a 1.0 M ammonium sulphate solution, buffered at pH 7.2, to a concentration of 5 mg/ml, and was layered on top of a 1.6 to 2.2 M ammonium sulphate solution. Crystals appeared within four to six weeks. They belong to space group C222 with cell dimensions a = 68.5 Angstrom, b = 100.5 Angstrom and c = 137.0 Angstrom, and diffract to at least 2.8 Angstrom resolution. There is one molecule with a molecule mass of 49,568 Da in the asymmetric unit.

KW - CRYSTALLIZATION

KW - PENICILLIN

KW - BINDING PROTEIN

KW - BETA-LACTAMASE

KW - MUREIN

KW - PEPTIDOGLYCAN

KW - REFINED CRYSTAL-STRUCTURE

KW - BACILLUS-LICHENIFORMIS

KW - NUCLEOTIDE-SEQUENCE

KW - NM RESOLUTION

KW - CRYSTALLIZATION

KW - ENZYME

KW - GENE

KW - BIOSYNTHESIS

KW - INHIBITION

KW - RESISTANCE

M3 - Comment/Letter to the editor

SN - 0022-2836

VL - 247

SP - 149

EP - 153

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 2

ER -

PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF PENICILLIN-BINDING PROTEIN-4 FROM ESCHERICHIA-COLI, A PROTEIN RELATED TO CLASS-A BETA-LACTAMASES

Abstract

Keywords

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