Crystal structure of the nucleosome core particle at 2.8 Å resolution

By K. Luger, A. Mäder, R. K. Richmond, D. Sargent, T. Richmond. 1997

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Histone Tails and the H3 αN Helix Regulate Nucleosome Mobility and Stability (2007, background): “The basic repeating unit of chromatin is the nucleosome core particle, which consists of 147 bp of DNA wrapped almost twice around an octamer of histone H2A, H2B, H3, and H4 proteins (12, 32).”
Review Histone Methylation: Dynamic or Static? (2002, background): “Of course, not all these states tions (Luger et al., 1997).”
Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. (2005, background): “The most fundamental unit of chromatin is the nucleosome, which is built from an octamer of core histones, H2A, H2B, H3, and H4, wrapped around 147 bp of DNA (Luger et al. 1997).”
Alteration of the nucleosomal DNA path in the crystal structure of a human nucleosome core particle (2005, methodology): “The crystal structure was determined by the molecular replacement method, using the previously published Xla-NCP structure (PDB entry 1AOI) (12) as a search model.”
The role of chromatin during transcription. (2007, background): “The nucleosome core is composed of 147 bp of DNA wrapped 1.65 turns around the histone octamer; there are 14 contact points between histones and DNA (Luger et al., 1997).”
Dot1p modulates silencing in yeast by methylation of the nucleosome core. (2002, unknown): “␣-helix 2 (Luger et al., 1997; White et al., 2001).”