Eukaryotic ribonucleases P and MRP are closely related RNA-based enzymes which contain a catalytic RNA component and several protein subunits. The roles of the protein subunits in the structure and function of eukaryotic ribonucleases P and MRP are not clear. Crystals of a complex that included a circularly permuted 46-nucleotide-long P3 domain of the RNA component of Saccharomyces cerevisiae ribonuclease MRP and selenomethionine derivatives of the shared ribonuclease P/MRP protein components Pop6 (18.2 kDa) and Pop7 (15.8 kDa) were obtained using the sitting-drop vapour-diffusion method. The crystals belonged to space group P4222 (unit-cell parameters a = b = 127.2, c = 76.8 Å, α = Β = γ = 90°) and diffracted to 3.25 Å resolution.
|Original language||English (US)|
|Number of pages||5|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|State||Published - Dec 25 2009|
All Science Journal Classification (ASJC) codes
- Structural Biology
- Condensed Matter Physics