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Crystallization and preliminary crystallographic studies of ribosome recycling factor from Escherichia coli.
- Source :
-
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2000 Jan; Vol. 56 (Pt 1), pp. 84-5. - Publication Year :
- 2000
-
Abstract
- Ribosome recycling factor (RRF) catalyzes the disassembly of a termination complex during the final stage of protein synthesis. RRF from Escherichia coli has been crystallized with PEG 400 as precipitant at 287 K. The crystal belongs to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell parameters a = b = 48.08, c = 141.67 A. Native data were collected from a frozen crystal to a resolution of 3.0 A on a Cu Kalpha rotating-anode X-ray source.
- Subjects :
- Bacterial Proteins genetics
Crystallization
Crystallography, X-Ray
Escherichia coli genetics
Gene Expression
Genes, Bacterial
Proteins genetics
Ribosomal Proteins
Ribosomes metabolism
Bacterial Proteins chemistry
Bacterial Proteins isolation & purification
Escherichia coli chemistry
Proteins chemistry
Proteins isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 0907-4449
- Volume :
- 56
- Issue :
- Pt 1
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section D, Biological crystallography
- Publication Type :
- Academic Journal
- Accession number :
- 10666636
- Full Text :
- https://doi.org/10.1107/s0907444999013906