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Purification, crystallization and preliminary X-ray diffraction analysis of Imp3 in complex with an Mpp10 peptide involved in yeast ribosome biogenesis
- Source :
- Acta crystallographica. Section F, Structural biology communications. 70(Pt 7)
- Publication Year :
- 2014
-
Abstract
- Eukaryotic ribosome synthesis requires a vast number of transiently associated factors. Mpp10, Imp3 and Imp4 form a protein complex in the 90S pre-ribosomal particle that conducts early processing of 18S rRNA. Here, a short fragment of Mpp10 was identified to associate with and increase the solubility of Imp3. An Imp3–Mpp10 complex was co-expressed, co-purified and co-crystallized. Preliminary X-ray diffraction analysis revealed that the crystal diffracted to 2.1 Å resolution and belonged to space groupP212121, with unit-cell parametersa= 51.6,b= 86.9,c= 88.7 Å.
- Subjects :
- Ribosomal Proteins
Saccharomyces cerevisiae Proteins
Stereochemistry
Recombinant Fusion Proteins
5.8S ribosomal RNA
Saccharomyces cerevisiae
Molecular Sequence Data
Biophysics
Ribosome biogenesis
Gene Expression
Crystallography, X-Ray
Biochemistry
Structural Biology
Genetics
Escherichia coli
Amino Acid Sequence
Cloning, Molecular
biology
Translation (biology)
Condensed Matter Physics
biology.organism_classification
Phosphoproteins
Yeast
Peptide Fragments
Molecular Weight
Crystallography
A-site
Ribonucleoproteins
Crystallization Communications
T arm
Eukaryotic Ribosome
Crystallization
Ribosomes
Protein Binding
Subjects
Details
- ISSN :
- 2053230X
- Volume :
- 70
- Issue :
- Pt 7
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section F, Structural biology communications
- Accession number :
- edsair.doi.dedup.....057f54b42f8de472651888fe8a1b3a74