title: Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast ribonuclease MRP in a complex with RNase P/MRP protein components Pop6 and Pop7.
abstract: 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 P4(2)22 (unit-cell parameters a = b = 127.2, c = 76.8 A, alpha = beta = gamma = 90 degrees ) and diffracted to 3.25 A resolution.
authors.affiliation: Department of Biochemistry and Molecular Biology, Pennsylvania State University, USA.
authors.forename: Anna
authors.initials: A
authors.lastname: Perederina
authors.forename: Olga
authors.initials: O
authors.lastname: Esakova
authors.forename: Chao
authors.initials: C
authors.lastname: Quan
authors.forename: Elena
authors.initials: E
authors.lastname: Khanova
authors.forename: Andrey S
authors.initials: AS
authors.lastname: Krasilnikov
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004722:Endoribonucleases / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D043262:Ribonuclease P / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000201:enzymology
chemical_list: D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; D043262:Ribonuclease P