Summary from the GEO: "From biosynthesis to assembly into nucleosomes, histones are handed through a cascade of histone chaperones, which shield histones from non-specific interactions. Whether mechanisms exist to safeguard the histone fold during histone chaperone handover events or to release trapped intermediates is unclear. Using structure-guided and functional proteomics, we identify and characterize...

This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes electron microscopy data identifying the crystal structure of DNAJC9 HBD helix2 in complex with H3.3-H4 dimer and MCM2 HBD. The main summary display for this entry includes information on the experimental method, validation, macromolecules and small molecules included in the deposit, as well as...

This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes electron microscopy data identifying the crystal structure of DNAJC9 HBD in complex with H3.3-H4 dimer and MCM2 HBD. The main summary display for this entry includes information on the experimental method, validation, macromolecules and small molecules included in the deposit, as well as version...

Description from PRIDE: "From biosynthesis to assembly into nucleosomes, histones are handed through a cascade of histone chaperones, which shield histones from non-specific interactions. Whether mechanisms exist to safeguard the histone fold during histone chaperone handover events or to release trapped intermediates is unclear. Using structure-guided and functional proteomics, we identify and characterize...

Raw data for Western blots, gel-based assays and ITC as a pdf. These images are correlated with the experiments and descriptions of the associated publication. Overall, research for the publication demonstrated that "DNAJC9 integrates ATP-resourced protein folding into the histone supply pathway to resolve aberrant intermediates throughout the dynamic lives of histones."