{"EMPIAR-11574":{"imagesets":[{"segmentations":[],"name":"Unaligned multi-frame micrographs of HIV-1 CA lattice templated on 30-nm liposomes in the presence of assembly cofactor IP6; bound to lenacapavir","directory":"data/templena_tif-frames_fixed","category":"micrographs - multiframe","header_format":"TIFF","data_format":"TIFF","num_images_or_tilt_series":696,"frames_per_image":50,"frame_range_min":null,"frame_range_max":null,"voxel_type":"UNSIGNED BYTE","pixel_width":0.655,"pixel_height":0.655,"micrographs_file_pattern":"data/templena_tif-frames_fixed/*.tif","picked_particles_file_pattern":"data/templena_tif-frames_fixed/run_data.star","picked_particles_directory":"","details":"'Raw,' unaligned multi-frame movies collected using a Talos Arctica microscope equipped with a Gatan K3 detector/BioQuantum energy filter operating in super-resolution mode.\n\nVoltage: 200 kV\nPhysical pixel size: 1.31Å/pixel\nTotal dose: 50 e-/Å^2\n\nGain reference (gain_ref.mrc) is included.\nPicked particle coordinates are provided in run_data.star.","image_width":"11520","image_height":"8184"}],"workflow_file":null,"grant_references":[{"funding_body":"National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)","code":"R01AI147890","country":"United States"}],"version_history":[],"title":"HIV-1 capsid lattice assembled on 30-nm liposome scaffolds in the presence of assembly cofactor IP6; bound to lenacapavir","principal_investigator":[{"author_orcid":"0000-0003-3693-2531","middle_name":"A","organization":"Cornell University","street":"360 Biotechnology Building, 526 Campus Road","town_or_city":"Ithaca","state_or_province":"New York","post_or_zip":"14853","telephone":null,"fax":null,"first_name":"Robert","last_name":"Dick","email":"rad82 [at] cornell.edu","country":"United States","entry":"EMPIAR-11574"}],"status":"REL","deposition_date":"2023-04-25","release_date":"2023-06-19","obsolete_date":null,"update_date":"2023-06-19","corresponding_author":{"author":{"author_orcid":"0000-0003-3693-2531","middle_name":"A","organization":"Cornell University","street":"360 Biotechnology Building, 526 Campus Road","town_or_city":"Ithaca","state_or_province":"New York","post_or_zip":"14853","first_name":"Robert","last_name":"Dick","country":"United States"}},"authors":[{"author":{"name":"Highland CMH","author_orcid":"0000-0003-4029-0113"}},{"author":{"name":"Dick RAD","author_orcid":"0000-0003-3693-2531"}}],"cross_references":["EMD-29776"],"biostudies_references":[],"idr_references":[],"empiar_references":[],"citation":[{"authors":[{"name":"Highland CM","author_orcid":"0000-0003-4029-0113"},{"name":"Tan A","author_orcid":"0000-0002-4046-7380"},{"name":"Ricaña CL","author_orcid":"0000-0002-9733-9136"},{"name":"Briggs JAG","author_orcid":"0000-0003-3990-6910"},{"name":"Dick RA","author_orcid":"0000-0003-3693-2531"}],"editors":[{"name":"Hurley JHH","author_orcid":"0000-0001-5054-5445"}],"published":true,"j_or_nj_citation":true,"title":"Structural insights into HIV-1 polyanion-dependent capsid lattice formation revealed by single particle cryo-EM","volume":"120","country":"United States","first_page":null,"last_page":null,"year":"2023","language":"English","doi":"10.1073/pnas.2220545120","pubmedid":"37094124","details":"ABSTRACT: The HIV-1 capsid houses the viral genome and interacts extensively with host cell proteins throughout the viral life cycle. It is composed of capsid protein (CA), which assembles into a conical fullerene lattice composed of roughly 200 CA hexamers and 12 CA pentamers. Previous structural analyses of individual CA hexamers and pentamers have provided valuable insight into capsid structure and function, but detailed structural information about these assemblies in the broader context of the capsid lattice is lacking. In this study, we combined cryoelectron tomography and single particle analysis (SPA) cryoelectron microscopy to determine structures of continuous regions of the capsid lattice containing both hexamers and pentamers. We also developed a method of liposome scaffold-based in vitro lattice assembly (“lattice templating”) that enabled us to directly study the lattice under a wider range of conditions than has previously been possible. Using this approach, we identified a critical role for inositol hexakisphosphate in pentamer formation and determined the structure of the CA lattice bound to the capsid-targeting antiretroviral drug GS-6207 (lenacapavir). Our work reveals key structural details of the mature HIV-1 CA lattice and establishes the combination of lattice templating and SPA as a robust strategy for studying retroviral capsid structure and capsid interactions with host proteins and antiviral compounds.","book_chapter_title":null,"publisher":null,"publication_location":null,"journal":"Proceedings of the National Academy of Sciences of the United States of America","journal_abbreviation":"Proc Natl Acad Sci U S A","issue":"18","preprint":false}],"dataset_size":"1.8 TB","experiment_type":"EMDB","scale":"molecule","related_pdb_entries":["8g6o"],"entry_doi":"10.6019/EMPIAR-11574"}}