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Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae.
Acta Crystallogr D Biol Crystallogr. 2004 May; 60(Pt 5):950-1.AC

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.

Authors+Show Affiliations

Riboldi-Tunnicliffe A
IBLS, Division of Infection and Immunity, University of Glasgow, Glasgow G12 8QQ, Scotland.
Trombe MC
No affiliation info available
Bent CJ
No affiliation info available
Isaacs NW
No affiliation info available
Mitchell TJ
No affiliation info available

MeSH

Bacterial ProteinsCloning, MolecularCrystallizationCrystallography, X-RayIntracellular Signaling Peptides and ProteinsMutationProtein ConformationRecombinant ProteinsStreptococcus pneumoniae

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15103149

Citation

Riboldi-Tunnicliffe, Alan, et al. "Crystallization and Preliminary Crystallographic Studies of the D59A Mutant of MicA, a YycF Response-regulator Homologue From Streptococcus Pneumoniae." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 5, 2004, pp. 950-1.
Riboldi-Tunnicliffe A, Trombe MC, Bent CJ, et al. Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 5):950-1.
Riboldi-Tunnicliffe, A., Trombe, M. C., Bent, C. J., Isaacs, N. W., & Mitchell, T. J. (2004). Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 5), 950-1.
Riboldi-Tunnicliffe A, et al. Crystallization and Preliminary Crystallographic Studies of the D59A Mutant of MicA, a YycF Response-regulator Homologue From Streptococcus Pneumoniae. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 5):950-1. PubMed PMID: 15103149.
* Article titles in AMA citation format should be in sentence-case
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, Y1 - 2004/04/21/ PY - 2004/02/09/received PY - 2004/03/11/accepted PY - 2004/4/23/pubmed PY - 2005/1/27/medline PY - 2004/4/23/entrez SP - 950 EP - 1 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 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. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15103149/Crystallization_and_preliminary_crystallographic_studies_of_the_D59A_mutant_of_MicA_a_YycF_response_regulator_homologue_from_Streptococcus_pneumoniae_ DB - PRIME DP - Unbound Medicine ER -