This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes cryogenic electron microscopy data identifying the Cryo-EM structure of AcrVIA1-Cas13(crRNA) complex. The main summary display for this entry includes information on the experimental method and validation, macromolecules and version history. Data is provided for download as FASTA sequence format,...

This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes electron microscopy data used for modeling the Cryo-EM structure of Cas13(crRNA). The main summary display for this entry includes information on the experimental data, validation, macromolecules and version history. Data is provided for download as FASTA sequence format, the Protein Data Bases...

This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes cryogenic electron microscopy data identifying the structure of human SHLD2-SHLD3-REV7-TRIP13(E253Q) complex. The main summary display for this entry includes information on the experimental method, validation, macromolecules and small molecules in the deposit, as well as entry history. Data...

This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes x-ray diffraction data identifying the crystal structure of human SHLD2-SHLD3-REV7 complex. The main summary display for this entry includes information on the experimental method, validation, macromolecules in the deposit, as well as entry history. Data is provided for download as FASTA sequence...

This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes x-ray diffraction data identifying the crystal structure of human REV7(R124A)-SHLD3(35-58) complex. The main summary display for this entry includes information on the experimental method, validation, macromolecules in the deposit, as well as entry history. Data is provided for download as FASTA...

Trimethylation of histone H3 lysine 4 (H3K4me3) is associated with transcriptional start sites and proposed to regulate transcription initiation. However, redundant functions of the H3K4 SET1/COMPASS methyltransferase complexes complicate elucidation of the specific role of H3K4me3 in transcriptional regulation. Here, we show that acute ablation of shared subunits of the SET1/COMPASS complexes leads...