Crystallization and preliminary X-ray study of an N-terminal fragment of rat liver ribosomal P2 protein
| Autor: | Richard Haser, Jean-Paul Reboud, David Mandelman, Jean Pierre Lavergne, Philippe Gonzalo, Catherine Corbier |
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| Rok vydání: | 2001 |
| Předmět: |
Ribosomal Proteins
Pentamer Eukaryotic Large Ribosomal Subunit Protein subunit Nucleation General Medicine Ribosomal RNA Biology Crystallography X-Ray Phosphoproteins law.invention Rats Elongation factor Crystallography Liver Structural Biology law Animals Orthorhombic crystal system Crystallization |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 58(Pt 4) |
| ISSN: | 0907-4449 |
| Popis: | Ribosomal P proteins have been shown to be involved in the binding of elongation factors and participate in factor-dependent GTP hydrolysis. The P proteins form the pentamer (P1/P2)(2)-P0 constituting the lateral flexible stalk of the 60S ribosomal subunit. The highly soluble domain (1-65) of rat liver P2 has been overexpressed in Escherichia coli as an N-terminal poly-His-tagged protein and crystallized. To reduce nucleation and improve crystal morphology and diffraction power, the crystals were grown in a gel matrix and an oil barrier was added between the reservoir and the drop to reduce the rate of vapour diffusion. This dramatically reduced the nucleation in the drops and yielded diffraction-quality crystals. Data were collected to 2.4 A resolution at beamline ID 14-1, ESRF. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 37.7, b = 96.7, c = 135.0 A. |
| Databáze: | OpenAIRE |
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