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The conformational flexibility of the C-terminus of histone H4 promotes histone octamer and nucleosome stability and yeast viability.

Myrriah S Chavez | Jean K Scorgie | Briana K Dennehey | Seth Noone | Jessica K Tyler | Mair Ea Churchill
Epigenetics & chromatin | 2012

The protein anti-silencing function 1 (Asf1) chaperones histones H3/H4 for assembly into nucleosomes every cell cycle as well as during DNA transcription and repair. Asf1 interacts directly with H4 through the C-terminal tail of H4, which itself interacts with the docking domain of H2A in the nucleosome. The structure of this region of the H4 C-terminus differs greatly in these two contexts.

Pubmed ID: 22541333

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Associated grants

  • Agency: NCI NIH HHS, United States
    Id: P30 CA046934
  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM064475
  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM079154

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Phaser (tool)

RRID:SCR_014219

Crystallographic software which solves structures using algorithms and automated rapid search calculations to perform molecular replacement and experimental phasing methods.

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ImageQuant (tool)

RRID:SCR_014246

Software for automatic general image analysis. It provides fully automatic analysis of 1-D gels including lane creation, background subtraction, band detection, molecular weight calibration, quantity calibration, and normalization. Editing tools are provided for cropping, rotating, and filtering images.

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CCP4 (tool)

RRID:SCR_007255

Portal for Macromolecular X-Ray Crystallography to produce and support an integrated suite of programs that allows researchers to determine macromolecular structures by X-ray crystallography, and other biophysical techniques. Used in the education and training of scientists in experimental structural biology for determination and analysis of protein structure.

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