Abstract
Ski7 (superkiller protein 7) plays a critical role in the mRNA surveillance pathway. The C-terminal fragment of Ski7 (residues 520-747) from Saccharomyces cerevisiae was heterologously expressed in Escherichia coli and purified to homogeneity. It was successfully crystallized and preliminary X-ray data were collected to 2.0Å resolution using synchrotron radiation. The crystal belonged to a trigonal space group, either P3121 or P3221, with unit-cell parameters a = b = 73.5, c = 83.6Å. The asymmetric unit contains one molecule of the C-terminal fragment of Ski7 with a corresponding crystal volume per protein mass (V M) of 2.61Å3Da-1 and a solvent content of 52.8% by volume. The merging R factor is 6.6%. Structure determination by MAD phasing is under way.
Original language | English |
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Pages (from-to) | 1252-1255 |
Number of pages | 4 |
Journal | Acta Crystallographica Section:F Structural Biology Communications |
Volume | 70 |
DOIs | |
Publication status | Published - 2014 Sept 1 |
Bibliographical note
Publisher Copyright:© 2014 International Union of Crystallography.
Keywords
- RNA degradation
- Saccharomyces cerevisiae
- Ski7
- mRNA surveillance
- nonstop decay
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics