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

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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 P4222 (unit-cell parameters a = b = 127.2, c = 76.8 Å, α = Β = γ = 90°) and diffracted to 3.25 Å resolution.

Original languageEnglish (US)
Pages (from-to)76-80
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number1
DOIs
StatePublished - Dec 25 2009

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Ribonuclease P
yeast
Crystallization
X-Ray Diffraction
Yeast
X ray diffraction analysis
Yeasts
Protein Subunits
RNA
crystallization
proteins
diffraction
Selenomethionine
saccharomyces
Catalytic RNA
Crystals
Proteins
x rays
nucleotides
crystals

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Cite this

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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 P4222 (unit-cell parameters a = b = 127.2, c = 76.8 {\AA}, α = Β = γ = 90°) and diffracted to 3.25 {\AA} resolution.",
author = "Anna Perederina and Olga Esakova and Chao Quan and Elena Khanova and Krasilnikov, {Andrey S.}",
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T1 - 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

AU - Perederina, Anna

AU - Esakova, Olga

AU - Quan, Chao

AU - Khanova, Elena

AU - Krasilnikov, Andrey S.

PY - 2009/12/25

Y1 - 2009/12/25

N2 - 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.

AB - 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.

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