4.0 Article

Purification, crystallization and preliminary X-ray diffraction analysis of Imp3 in complex with an Mpp10 peptide involved in yeast ribosome biogenesis

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INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X14010905

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Funding

  1. National Natural Science Foundation of China [31325007]
  2. Ministry of Science and Technology of China [2010CB835402]
  3. Beijing Municipal Government

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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 angstrom resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 51.6, b = 86.9, c = 88.7 angstrom.

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