Crystallization and preliminary crystallographic studies on the chromo shadow domain (CSD) of mouse heterochromatin protein M31.
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.
Gao
Yu
Y
Laboratory of Structural Biology and MOE Laboratory of Protein Science School of Life Science and Engineering, Tsinghua University, Beijing 100084, People's Republic of China.
Ding
Yi
Y
Singh
Prim B
PB
Rao
Zihe
Z
D000818:Animals; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D051379:Mice; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry
C096188:Cbx1 protein, mouse; D002868:Chromosomal Proteins, Non-Histone; D010446:Peptide Fragments; D011994:Recombinant Proteins