Expression, purification and X-ray characterization of residues 18-230 from the pneumococcal histidine triad protein A (PhtA) from Streptococcus pneumoniae

Alan Riboldi-Tunnicliffe; Colin J Bent; Neil W Isaacs; Timothy J Mitchell

doi:10.1107/S0907444904004573

Expression, purification and X-ray characterization of residues 18-230 from the pneumococcal histidine triad protein A (PhtA) from Streptococcus pneumoniae

Alan Riboldi-Tunnicliffe, Colin J Bent, Neil W Isaacs, Timothy J Mitchell

Microbiology and Infection

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9 Citations (Scopus)

Abstract

A fragment of the Streptococcus pneumoniae PhtA gene product (residues 18-230) was cloned and overexpressed in Escherichia coli. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 62.19, b = 35.9, c = 72.54 A, beta = 90.01 degrees. The crystals diffract X-rays to beyond 1.2 A resolution.

Original language	English
Pages (from-to)	926-8
Number of pages	3
Journal	Acta Crystallographica Section D Biological Crystallography
Volume	60
Issue number	Pt 5
DOIs	https://doi.org/10.1107/S0907444904004573
Publication status	Published - May 2004

Keywords

Crystallization
Crystallography, X-Ray
Escherichia coli
Hydrolases
Peptide Fragments
Protein Conformation
Recombinant Proteins
Streptococcus pneumoniae

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title = "Expression, purification and X-ray characterization of residues 18-230 from the pneumococcal histidine triad protein A (PhtA) from Streptococcus pneumoniae",

abstract = "A fragment of the Streptococcus pneumoniae PhtA gene product (residues 18-230) was cloned and overexpressed in Escherichia coli. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 62.19, b = 35.9, c = 72.54 A, beta = 90.01 degrees. The crystals diffract X-rays to beyond 1.2 A resolution.",

keywords = "Crystallization, Crystallography, X-Ray, Escherichia coli, Hydrolases, Peptide Fragments, Protein Conformation, Recombinant Proteins, Streptococcus pneumoniae",

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year = "2004",

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journal = "Acta Crystallographica Section D Biological Crystallography",

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}

Expression, purification and X-ray characterization of residues 18-230 from the pneumococcal histidine triad protein A (PhtA) from Streptococcus pneumoniae. / Riboldi-Tunnicliffe, Alan; Bent, Colin J; Isaacs, Neil W et al.
In: Acta Crystallographica Section D Biological Crystallography, Vol. 60, No. Pt 5, 05.2004, p. 926-8.

Research output: Contribution to journal › Article › peer-review

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T1 - Expression, purification and X-ray characterization of residues 18-230 from the pneumococcal histidine triad protein A (PhtA) from Streptococcus pneumoniae

AU - Riboldi-Tunnicliffe, Alan

AU - Bent, Colin J

AU - Isaacs, Neil W

AU - Mitchell, Timothy J

PY - 2004/5

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AB - A fragment of the Streptococcus pneumoniae PhtA gene product (residues 18-230) was cloned and overexpressed in Escherichia coli. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 62.19, b = 35.9, c = 72.54 A, beta = 90.01 degrees. The crystals diffract X-rays to beyond 1.2 A resolution.

KW - Crystallization

KW - Crystallography, X-Ray

KW - Escherichia coli

KW - Hydrolases

KW - Peptide Fragments

KW - Protein Conformation

KW - Recombinant Proteins

KW - Streptococcus pneumoniae

U2 - 10.1107/S0907444904004573

DO - 10.1107/S0907444904004573

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SN - 0907-4449

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EP - 928

JO - Acta Crystallographica Section D Biological Crystallography

JF - Acta Crystallographica Section D Biological Crystallography

IS - Pt 5

ER -

Expression, purification and X-ray characterization of residues 18-230 from the pneumococcal histidine triad protein A (PhtA) from Streptococcus pneumoniae

Abstract

Keywords

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