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Crystallization and preliminary crystallographic studies of the D59A mutant of MicA, a YycF response-regulator homologue from Streptococcus pneumoniae.
- Source :
-
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2004 May; Vol. 60 (Pt 5), pp. 950-1. Date of Electronic Publication: 2004 Apr 21. - Publication Year :
- 2004
-
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.
- Subjects :
- Bacterial Proteins chemistry
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Intracellular Signaling Peptides and Proteins genetics
Intracellular Signaling Peptides and Proteins isolation & purification
Mutation
Protein Conformation
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Intracellular Signaling Peptides and Proteins chemistry
Streptococcus pneumoniae chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0907-4449
- Volume :
- 60
- Issue :
- Pt 5
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section D, Biological crystallography
- Publication Type :
- Academic Journal
- Accession number :
- 15103149
- Full Text :
- https://doi.org/10.1107/S0907444904005712