Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae

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

doi:10.1107/S0907444904005712

Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae

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

Microbes, Infections and Microbiomes

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3 Citations (Scopus)

Abstract

RR02 (MicA) is an essential bacterial protein that belongs to the YycF family of response regulators and consists of two domains: an N-terminal receiver domain and a C-terminal effector domain. Streptococcus pneumoniae RR02 (MicA; residues 2-234) has been crystallized using the sitting-drop vapour-diffusion technique. The crystals belong to space group P2(1), with unit-cell parameters a = 46.46, b = 32.61, c = 63.35 A, beta = 90.01 degrees. X-ray diffraction data have been collected to 1.93 A resolution.

Original language	English
Pages (from-to)	950-1
Number of pages	2
Journal	Acta Crystallographica Section D Biological Crystallography
Volume	60
Issue number	Pt 5
DOIs	https://doi.org/10.1107/S0907444904005712
Publication status	Published - May 2004

Keywords

Bacterial Proteins
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Intracellular Signaling Peptides and Proteins
Mutation
Protein Conformation
Recombinant Proteins
Streptococcus pneumoniae

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title = "Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae",

abstract = "RR02 (MicA) is an essential bacterial protein that belongs to the YycF family of response regulators and consists of two domains: an N-terminal receiver domain and a C-terminal effector domain. Streptococcus pneumoniae RR02 (MicA; residues 2-234) has been crystallized using the sitting-drop vapour-diffusion technique. The crystals belong to space group P2(1), with unit-cell parameters a = 46.46, b = 32.61, c = 63.35 A, beta = 90.01 degrees. X-ray diffraction data have been collected to 1.93 A resolution.",

keywords = "Bacterial Proteins, Cloning, Molecular, Crystallization, Crystallography, X-Ray, Intracellular Signaling Peptides and Proteins, Mutation, Protein Conformation, Recombinant Proteins, Streptococcus pneumoniae",

author = "Alan Riboldi-Tunnicliffe and Trombe, {Marie Claude} and Bent, {Colin J} and Isaacs, {Neil W} and Mitchell, {Timothy J}",

year = "2004",

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doi = "10.1107/S0907444904005712",

language = "English",

volume = "60",

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journal = "Acta Crystallographica Section D Biological Crystallography",

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publisher = "International Union of Crystallography",

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Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae. / Riboldi-Tunnicliffe, Alan; Trombe, Marie Claude; Bent, Colin J et al.
In: Acta Crystallographica Section D Biological Crystallography, Vol. 60, No. Pt 5, 05.2004, p. 950-1.

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

TY - JOUR

T1 - Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae

AU - Riboldi-Tunnicliffe, Alan

AU - Trombe, Marie Claude

AU - Bent, Colin J

AU - Isaacs, Neil W

AU - Mitchell, Timothy J

PY - 2004/5

Y1 - 2004/5

N2 - RR02 (MicA) is an essential bacterial protein that belongs to the YycF family of response regulators and consists of two domains: an N-terminal receiver domain and a C-terminal effector domain. Streptococcus pneumoniae RR02 (MicA; residues 2-234) has been crystallized using the sitting-drop vapour-diffusion technique. The crystals belong to space group P2(1), with unit-cell parameters a = 46.46, b = 32.61, c = 63.35 A, beta = 90.01 degrees. X-ray diffraction data have been collected to 1.93 A resolution.

AB - RR02 (MicA) is an essential bacterial protein that belongs to the YycF family of response regulators and consists of two domains: an N-terminal receiver domain and a C-terminal effector domain. Streptococcus pneumoniae RR02 (MicA; residues 2-234) has been crystallized using the sitting-drop vapour-diffusion technique. The crystals belong to space group P2(1), with unit-cell parameters a = 46.46, b = 32.61, c = 63.35 A, beta = 90.01 degrees. X-ray diffraction data have been collected to 1.93 A resolution.

KW - Bacterial Proteins

KW - Cloning, Molecular

KW - Crystallization

KW - Crystallography, X-Ray

KW - Intracellular Signaling Peptides and Proteins

KW - Mutation

KW - Protein Conformation

KW - Recombinant Proteins

KW - Streptococcus pneumoniae

U2 - 10.1107/S0907444904005712

DO - 10.1107/S0907444904005712

M3 - Article

C2 - 15103149

SN - 0907-4449

VL - 60

SP - 950

EP - 951

JO - Acta Crystallographica Section D Biological Crystallography

JF - Acta Crystallographica Section D Biological Crystallography

IS - Pt 5

ER -

Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae

Abstract

Keywords

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