Crystallization and preliminary crystallographic studies on the chromo shadow domain (CSD) of mouse heterochromatin protein M31

Yu Gao, Yi Ding, Prim B Singh, Zihe Rao

Research output: Contribution to journalArticle

Abstract

Members of the heterochromatin protein 1 (HP1) class of non-histone chromosomal proteins are components of heterochromatin and are involved in the epigenetic regulation of the genome. HP1 proteins are modular and consist of two sequence-related domains called the chromodomain (CD) and the chromo shadow domain (CSD). In order to investigate the role of the murine HP1-like protein M31 in heterochromatin formation and gene silencing, recombinant CSD was overexpressed in Escherichia coli and crystallized using the hanging-drop vapour-diffusion method with PEG 4000 as precipitant. Diffraction data to 2.9 A were collected from a native crystal belonging to space group C222(1), with unit-cell parameters a = 60.0, b = 95.6, c = 91.7 A, alpha = beta = gamma = 90 degrees.

Original languageEnglish
Pages (from-to)1051-3
Number of pages3
JournalActa Crystallographica Section D: Structural Biology
Volume58
Issue numberPt 6 Pt 2
Publication statusPublished - Jun 2002

Keywords

  • Animals
  • Chromosomal Proteins, Non-Histone
  • Crystallization
  • Crystallography, X-Ray
  • Mice
  • Peptide Fragments
  • Protein Conformation
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Journal Article
  • Research Support, Non-U.S. Gov't

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