FAQ
EM map deposition questions
- How do I begin a map deposition to EMDB?
- What map formats are accepted by EMDB?
- What is the difference between a deposition session id and an EMDB accession id?
- We have two maps for one submitted manuscript, one native, one with cofactor protein. Do we need to complete two separate depositions?
- Can I deposit a composite map to EMDB?
- How can we deposit multiple 3D volumes generated from imaging of a single specimen?
- How can I request a change/correction/citation update to my EMDB entry?
- Our manuscript has not been officially accepted yet, so please do not release our entry.
- I received an email stating that my map is being released. When will it be available in the EM Data Bank?
- The journal I am targetting requires editors and referees access to the structure while my manuscript is under review. Does EMDB provide confidential access to editors or referees if a structure is "on hold"?
EM map-derived coordinate model deposition questions
- I have fitted coordinates for my map, can I include them with my map entry?
- I obtained coordinates from PDB and used rigid-body fitting to place them into my map. Can I deposit these coordinates to PDB?
- My fitted coordinates correspond to a protein homolog. During the PDB deposition, should I provide the species information/sequence information for the EM sample or for the protein homolog?
- How are coordinates derived from EM reconstructions validated?
- We have a new coordinate model fitted into an EMDB map entry authored by another research group. Can we deposit our coordinates?
EM map, model and metadata access questions
- How can I find/download a map or browse the EMDB database?
- How can I view EMDB maps?
- How can I download a map that has already been deposited and released?
- Can I use maps and/or map images from EMDB in my thesis/publication?
- How can I download EMDB map entry metadata?
EM map deposition answers
How do I begin a map deposition to EMDB?
EMDB maps can be deposited through the wwPDB OneDep system. Tutorials for which can be found here.
What map formats are accepted by EMDB?
Maps can be deposited in mrc and ccp4 formats; they are converted to standard ccp4 format for redistribution in the EMDB.
What is the difference between a deposition session id and an EMDB accession id ?
When you initiate a deposition session you are assigned a session id (reference code). The session id is a "private" identifier known only to the depositor and the deposition site. When you complete your deposition and submit it to the EMDB, you are assigned a public accession code ("EMD-" followed by a four or five digit number). The public accession code is the id you should provide to journals when indicating your EMDB submission; it is also the code by which you can access to your entry in the publicly available EMDB search and atlas pages.
We have two maps for one submitted manuscript, one native, one with cofactor protein. Do we need to complete two separate depositions?
If the maps were generated from different specimen preparations/imaging experiments you will need to make two separate depositions.
Time saving tip: complete the submission for the first map (deposition session 1), and then for the second map (deposition session 2) select the option "based on previous submission." You will need to provide the 1st deposition session id and password in order to use this option.
Can I deposit a composite map to EMDB?
A composite map is here defined as a map constructed by piecing together two or more experimentally derived component EM maps together. A composite map may be deposited to EMDB if the component maps share the same specimen preparations/imaging experiments (see also "We have two maps for one submitted manuscript, one native, one with cofactor protein. Do we need to complete two separate depositions?”). For composite map depositions we ask that you: a) also provide each of the component maps as individual EMDB entries, in addition to the composite map entry; b) add the following suffix to the composite map entry title: “(composite structure).”
How can we deposit multiple 3D volumes generated from imaging of a single specimen?
EM reconstruction methods are beginning to yield ensembles of maps representing multiple conformations/enzymatic states within a heterogeneous population of imaged particles. If you need to deposit multiple maps of this type you can do so either within a single submission, in which case one map must be designated at the primary map, or a separate submissions (please see answer above).
How can I request a change/correction/citation update to my EMDB entry?
Please log into your OneDep deposition and make the request using the communication module.
Our manuscript has not been officially accepted yet, so please do not release our entry.
The only part of an EMDB submission that is released immediately is the experimental information in the header. The header information will only be released after you have had an opportunity to comment on the curated data. The map will not be released until the hold period has elapsed which can be on publication (HPUB), or 1 year from deposition. The map will only be released immediately if you have requested this at the release option stage.
I received an email stating that my map is being released. When will it be available in the EM Data Bank?
EMDB follows the same weekly release cycle as PDB. Maps queued for release before Thursday at 5pm (UK) will be available from EMDB on the following Wednesday.
The journal I am targeting requires editors and referees access to the structure while my manuscript is under review. Does EMDB provide confidential access to editors or referees if a structure is "on hold"?
Unreleased structural data on hold, both maps and coordinate sets, are kept strictly confidential. After deposition, you will immediately receive EMDB ids for your map entries and PDB ids for your map-derived model entries, which you may include in your manuscript. In addition, for PDB model entries you can obtain validation reports that provide assessments of model quality while keeping the coordinate file confidential. We encourage journal editors and referees to request validation reports from depositors as part of the manuscript submission and review process. The reports are date-stamped, and display the wwPDB processing site logo. For more information see https://www.wwpdb.org/validation.html.
EM map-derived coordinate model deposition answers
I have fitted coordinates for my map, can I include them with my map entry?
Fitted coordinate models for EM entries may be deposited along with your map; they will be assigned a PDB id.
I obtained coordinates from PDB and used rigid-body fitting to place them into my map. Can I deposit these coordinates to PDB?
You can deposit coordinates derived from any fitting protocol, including rigid-body fitting, flexible fitting, or de novo tracing. The deposited coordinates must be aligned and in-frame with the map.
My fitted coordinates correspond to a protein homolog. During the PDB deposition, should I provide the species information/sequence information for the EM sample or for the protein homolog?
The species information should correspond to your EM sample, but the sequence information should correspond to the protein homolog/fitted model.
How are coordinates derived from EM reconstructions validated?
Currently, model fit to an EMDB map is validated through visual inspection of the deposited map + model pair using a 3D graphics program. Models are also checked for correct stereochemistry and clashes; a validation report is issued for every submitted model.
We have a new coordinate model fitted into an EMDB map entry authored by another research group. Can we deposit our coordinates?
Yes, you can deposit your coordinates. Provide the EMDB map accession id (EMD-XXXX) as the associated EM volume of your coordinate deposition. The PDB policy regarding re-refined entries applies: "A re-refined entry may be deposited prior to publication but will not be processed (will have REFI status) or released until the associated publication has become publicly available." No changes will be made to the EMDB map entry.
EM map, model and metadata access answers
How can I find/download a map or browse the EMDB archive?
You can use the advanced search link on the top of the page.
To view the map on your own computer, you will first need to download the map from the EMDB atlas page and view the map with locally installed software. ChimeraX, Pymol, Coot (v. 0.6.2 or later), and other graphics programs can display EMDB maps when loaded as "ccp4" format maps.
How can I download a map that has already been deposited and released?
Released maps can be downloaded either from the 'downloads' tab of the atlas page for the entry or from one of the three wwPDB ftp distribution sites: ftp://ftp.ebi.ac.uk/pub/databases/emdb, https://ftp.wwpdb.org/pub/emdb or https://data.pdbj.org/pub/emdb. Some strategies to retrieve files from the ftp sites are posted here: https://www.wwpdb.org/download/downloads.php
Can I use maps and/or map images from EMDB in my thesis/publication?
Data files contained in the EMDB are free of all copyright restrictions and made fully and freely available for both non-commercial and commercial use. Users of the data should attribute the original authors of the structural data and the EMDB accession id. Many of the static EM map images shown on atlas pages have been contributed by the original deposition authors in which case they may also be protected by copyright law, even though we provide free access to them. The respective copyright holders of author-provided images retain rights for reproduction, redistribution and reuse. Users are responsible for compliance with copyright restrictions and are expected to adhere to the terms and conditions defined by the copyright holder.
How can I download EMDB map entry metadata?
The EMDB is distributed as a branch of the wwPDB archive, and is available via all of the wwPDB ftp sites. Instructions to retrieve EMDB xml metadata files are posted here: https://www.wwpdb.org/download/downloads.php
Quick links
Recent Entries
(Show all)Heteromeric GluA1/A2 in the activated state, amino-terminal domain (ATD)
Heteromeric GluA1/A2 in the activated state, ligand binding domain (LBD)
Heteromeric GluA1/A2-CNIH1 in the activated state, consensus refinement of LBD-TMD
Heteromeric GluA1/A2 in the desensitized state, composite map of ATD-LBD-TMD
Heteromeric GluA1/A2 in the desensitized state, amino-terminal domain (ATD)
Heteromeric GluA1/A2 in the desensitized state, consensus refinement of ATD-LBD-TMD
Heteromeric GluA1/A2-CNIH1 in the activated state, composite map of LBD-TMD
Composite map of GluA1/A2 in the activated state, in complex with positive allosteric modulator (R,R)-2b and agonist glutamate (ATD-LBD-TMD)
The helicase-primase complex from HHV1 bound with ssDNA and amenamevir
The primase module of the helicase-primase complex from HHV1 bound with ssDNA and amenamevir
The helicase module of the helicase-primase complex from HHV1 bound with ssDNA and amenamevir
The helicase module of the helicase-primase complex from HHV1 bound with ssDNA and pritelivir
The helicase-primase complex from HHV1 bound with ssDNA and pritelivir
The Primase module of the helicase-primase complex from HHV1 bound with ssDNA and pritelivir
Multibody refinement cryo-EM density map of the apex of the Saccharomyces cerevisiae KMN junction complex
Cryo-EM structure of the Saccharomyces cerevisiae KMN junction complex containing the Mis12c(Mtw1c) head 2 domain
Mutlbody refinement cryo-EM density map of the base of the Saccharomyces cerevisiae KMN junction complex
Consensus cryo-EM map of the Saccharomyces cerevisiae KMN junction complex lacking the Mis12c(Mtw1c) head 2 domain
Composite cryo-EM density map of the Saccharomyces cerevisiae KMN junction complex lacking the Mis12c(Mtw1c) head 2 domain
Multibody refinement cryo-EM density map of the base of the Saccharomyces cerevisiae KMN junction complex with Mis12c(Mtw1c) head 2 domain resolved
A broad-spectrum neutralizing antibody targeting the F protein of NiV and HeV
LY334370-bound serotonin 1F (5-HT1F) receptor-miniGoA protein complex
Structure of human cardiac sodium channel Nav1.5 in intermediate open state
Rat 80S ribosome purified from brain RNA granules at 10 mM Magnesium. Class 2 80S with PP tRNA
Rat 80S ribosome purified from brain RNA granules at 10 mM Magnesium. Class 1 80S with AP and PE tRNAs
MBP-maltose bound to distal DARPin (AHIR dodecamer scaffold system from split dataset with 6500 micrographs)
MBP-maltose bound to distal DARPin (AHIR dodecamer scaffold system from split dataset with 2500 micrographs)
MBP-maltose bound to distal DARPin (AHIR dodecamer scaffold system from split dataset with 8500 micrographs)
Focused refinement of PP2Ac repeats 2 and 3 of the CCDC6-PP2Ac complex
MBP-maltose bound to distal DARPin (AHIR dodecamer scaffold system from split dataset with 7500 micrographs)
MBP-maltose bound to distal DARPin (AHIR dodecamer scaffold system from split dataset with 500 micrographs)
MBP-maltose bound to distal DARPin (AHIR dodecamer scaffold system from split dataset with 8694 micrographs)
MBP-maltose bound to distal DARPin (AHIR dodecamer scaffold system from split dataset with 3500 micrographs)
MBP-maltose bound to distal DARPin (AHIR dodecamer scaffold system from split dataset with 5500 micrographs)
MBP-maltose bound to distal DARPin (AHIR dodecamer scaffold system from split dataset with 4500 micrographs)
Focused refinement of PP2Ac repeats 1 and 2 of the CCDC6-PP2Ac complex
MBP-maltose bound to distal DARPin (AHIR dodecamer scaffold system from split dataset with 1500 micrographs)
Focused refinement of PP2Ac repeats 3 and 4 of the CCDC6-PP2Ac complex
Composite structure of AP-2 bound to the dileucine motif and WxxPhi motif of CCDC32
Structure of AP-2 bound to the dileucine motif of CCDC32; consensus refinement
Structure of AP-2 bound to the dileucine motif and WxxPhi motif of CCDC32; focused refinement 3
Structure of AP-2 bound to the dileucine motif and WxxPhi motif of CCDC32; focused refinement 2
Structure of AP-2 bound to the dileucine motif of CCDC32; combined map
Structure of AP-2 bound to the dileucine motif and WxxPhi motif of CCDC32; consensus refinement
Structure of AP-2 bound to the dileucine motif of CCDC32; focused refinement
Structure of AP-2 bound to the dileucine motif and WxxPhi motif of CCDC32; focused refinement 1
Dimer of ATPase BrxC containing a Walker B mutation and bound to ATP from the Acinetobacter BREX system
Volume of PglZ in complex with BrxB-BrxC fusion from the Acinetobacter BREX system
Population B fibril generated from the Heterotypic interaction of Abeta40 and Medin.
Population A fibril generated from the Heterotypic interaction of Abeta40 and Medin.
Medin fibril generated from the heterotypic interaction of Abeta40 and Medin.
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, focused on UBE2D3+UHRF1 RING
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, focused on NLRP14+UHRF1
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, focused on PADI6 dimers 5
Native structure of cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, focused on PADI6 dimers 1-4
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, focused on NLRP4F
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, focused on NLRP5+TLE6+OOEP+KHDC3
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, consensus map
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, focused on tubulin
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, focused on FBXW19+FBXW21
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, focused on NLRP5+TLE6+OOEP+ZBED3+FBXW18
Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs, focused on NLRP14+UHRF1+UBE2D3
ZZ1-SO2H-induced assembly of the YPEL5-CTLH E3 ligase and BRD4(BD1) neosubstrate
Cryo-EM structure of human TRPV3 in complex with sevoflurane determined in MSP2N2 nanodisc
Ternary complex of a charged molecular glue degrader ZZ1-SO2H, BRD4(BD1) neosubstrate, and the CTLH E3 ligase receptor module YPEL5-WDR26
Ternary complex of an improved charged molecular glue degrader ZZ2-SO2H, BRD4(BD1) neosubstrate, and the CTLH E3 ligase receptor module YPEL5-WDR26
Translocation Module of the Peptide-Loading Complex Arrested by HCMV US6
Editing Module 1 of the Peptide-Loading Complex Arrested by HCMV US6
Heterodimeric ABC exporter TmrAB (wild type) in ATP-bound outward-facing occluded conformation in the absence of Mg2+
Central Tapasin Scaffold of the Peptide-Loading Complex Arrested by HCMV US6
Editing Module 2 of the Peptide-Loading Complex Arrested by HCMV US6
Structure of the YbjP lipoprotein bound to the AcrABZ-TolC efflux pump
Heterodimeric ABC exporter TmrAB (EQ mutant) in ATP-bound outward-facing occluded conformation in the absence of Mg2+
Cryo-EM structure of Rubisco with hetero small subunit 1A3B form I
Cryo-EM structure of Rubisco with hetero small subunit 1A3B form II
Cryo-EM structure of Escherichia coli transcription initiation complex with GpA and pseudouridimycin (PUM)
Cryo-EM structure of human beta-cardiac myosin bound to omecamtiv mecarbil in the interacting-heads motif and S2-FH docked state
Cryo-EM structure of Escherichia coli transcription initiation complex with GpA and des-hydroxy pseudouridimycin (des-hydroxy PUM)
Cryo-EM structure of human beta-cardiac myosin in the interacting-heads motif and S2-FH docked state
Cryo-EM structure of human beta-cardiac myosin bound to mavacamten in the interacting-heads motif and S2-FH docked state
Cryo-EM structure of human beta-cardiac myosin bound to mavacamten in the interacting-heads motif and S2-FH undocked state
Cryo-EM structure of human beta-cardiac myosin bound to omecamtiv mecarbil in the interacting-heads motif and S2-FH undocked state
Cryo-EM structure of human beta-cardiac myosin in the interacting-heads motif and S2-FH undocked state
CRYO-EM STRUCTURE OF THE A149T DIMER VARIANT OF SERINE HYDROXYMETHYLTRANSFERASE 8 FROM SOYBEAN CULTIVAR ESSEX IN COMPLEX WITH PLP
Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT
Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C3 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT
Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Influenza A virus Hemagglutinin (A/California/04/2009 H1N1), E47K HA2 stabilizing mutation (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT
Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C3 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Influenza A virus Hemagglutinin (A/California/04/2009 H1N1), E47K HA2 stabilizing mutation (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C3 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT
Influenza A virus Hemagglutinin (A/California/04/2009 H1N1), E47K HA2 stabilizing mutation (C3 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT
Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT
Azotobacter vinelandii MoFeP (C2 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT
Azotobacter vinelandii MoFeP (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT
Influenza A virus Hemagglutinin (A/California/04/2009 H1N1), E47K HA2 stabilizing mutation (C3 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Azotobacter vinelandii MoFeP (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Azotobacter vinelandii MoFeP (C2 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Rabbit muscle Aldolase (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Rabbit muscle Aldolase (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT
Azotobacter vinelandii MoFeP (C2 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT
Rabbit muscle Aldolase (D2 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT
Azotobacter vinelandii MoFeP (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT
Rabbit muscle Aldolase (D2 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Rabbit muscle Aldolase (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.5x SurfACT
Rabbit muscle Aldolase (D2 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT
Rabbit muscle Aldolase (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT
Rabbit muscle Aldolase (D2 symmetry) determined using the SPT Labtech chameleon in the presence of 0.5x SurfACT
Rabbit muscle Aldolase (C1 symmetry) determined using the SPT Labtech chameleon (gold-coated grids) in the presence of 1x SurfACT
Rabbit muscle Aldolase (C1 symmetry; subtomogram averaged; bottom air-water interface) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Rabbit muscle Aldolase (D2 symmetry) determined using a manually-operated plunging device in the presence of 0.25x SurfACT
Rabbit muscle Aldolase (C1 symmetry) determined using the TFS Vitrobot Mark IV in the presence of 1x SurfACT
Rabbit muscle Aldolase (D2 symmetry) determined using the SPT Labtech chameleon (gold-coated grids) in the presence of 1x SurfACT
Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C3 symmetry; subtomogram averaged) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Influenza A virus Hemagglutinin (A/Darwin/6/2021 H3N2) (C3 symmetry; subtomogram averaged) determined using the SPT Labtech chameleon in the presence of 0x SurfACT
Rabbit muscle Aldolase (D2 symmetry) determined using the TFS Vitrobot Mark IV in the presence of 0x SurfACT
Rabbit muscle Aldolase (C1 symmetry; subtomogram averaged) determined using the SPT Labtech chameleon in the presence of 0x SurfACT
Rabbit muscle Aldolase (D2 symmetry) determined using the TFS Vitrobot Mark IV in the presence of 1x SurfACT
Rabbit muscle Aldolase (C1 symmetry; subtomogram averaged) determined using the SPT Labtech chameleon in the presence of 1x SurfACT
Rabbit muscle Aldolase (C1 symmetry) determined using the TFS Vitrobot Mark IV in the presence of 0x SurfACT
Rabbit muscle Aldolase (C1 symmetry) determined using a manually-operated plunging device in the presence of 0.25x SurfACT
Rabbit muscle Aldolase (C1 symmetry; subtomogram averaged; top air-water interface) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Rabbit muscle Aldolase (C1 symmetry; subtomogram averaged; center ice) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Rabbit muscle Aldolase (C1 symmetry; subtomogram averaged) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT
Avian TRPM8 (Parus major) menthol bound structure resolved in cell vesicles using cryo-EM
Avian TRPM8 (Parus major) semi-swapped, calcium free, menthol bound structure resolved in cell vesicles
Parus major TRPM8, fully-swapped state determined in the presence of menthol
Avian TRPM8 (Parus major) "undetermined" class 1 resolved in cell vesicles using cryo-EM
Human TRPM8 (wild-type) semi-swapped structure, calcium-free, 4 degress Celsius, determined using cell vesicles
Human TRPM8 V915Y semi-swapped structure, cold in the presence of calcium, determined using GDN
Avian TRPM8 (Parus major) "undetermined" class 2 resolved in cell vesicles using cryo-EM
The cryo-EM structure of Pakpunavirus P7-1 empty particle neck (portal:H-t-T)
Dimer of BrxC-BrxB fusion complexed with PglZ from the Acinetobacter BREX system
Structure of ATD truncated glutamate receptor mGluD1 complexed with GABA and Calcium
Structure of the A654C substituted ionotropic glutamate receptor mGluD1
Structure of ATD truncated glutamate receptor mGluD1 complexed with D-serine
Structure of ionotropic glutamate receptor mGluD1 complexed with D-serine
The cryo-EM structure of human Piezo2-MDFIC2 complex (cap focused map)
The cryo-EM structure of human Piezo2-MDFIC complex (consensus map)
The cryo-EM structure of human Piezo2-MDFIC2 complex (blade focused map)
The cryo-EM structure of human Piezo2-MDFIC complex (cap focused map)
The cryo-EM structure of human Piezo2-MDFIC2 complex (consensus map)
The cryo-EM structure of human Piezo2-MDFIC2 complex (composite map)
The cryo-EM structure of human Piezo2-MDFIC complex (blade focused map)
The cryo-EM structure of human Piezo2-MDFIC complex (composite map)
CryoEM structure of coxsackievirus B1 virus-like particle with VP4 deletion
Cryo-EM structure of cyanobacterial bicarbonate transporter CmpBCD in the presence of nitrate
Cryo-EM structure of cyanobacterial bicarbonate transporter CmpBCD in complex with ATP
Helical Reconstruction of DENV2 THSTI/TRC/01 tubular particles bound with D14.F25.S02 fab
Cryo-EM structure of formate dehydrogenase from Shewanella oneidensis MR-1 (SoFdhAB)
Cryo-electron tomogram of cyanobacterium Anabaena sp. PCC 7120 with putative CorM filaments (Isonet-processed)
Cryo-electron tomogram of delta-cse mutant cyanobacterium Anabaena sp. PCC 7120 with putative CorM filaments
Cryo-EM structure of the CorM filament from cyanobacterium Anabaena sp. PCC 7120
Cryo-EM structure of human sodium/proton antiporter NHE1 in complex with Cariporide in an outward-open conformation
Structure of glycosylphosphatidylinositol transamidase,state 1,unsharpened map
Cryo-EM structure of human sodium/proton antiporter NHE1 in complex with Rimeporide in an outward-open conformation
Cryo-EM structure of the CorM filament in the presence of CorR from cyanobacterium Anabaena sp. PCC 7120
Cryo-EM structure of human sodium/proton antiporter NHE1 in complex with Eniporide in an outward-open conformation
CryoEM structure of human DNMT1 (aa 698-1616) in complex with hemimethylated dsDNA and inhibitor DMT207
Cryo-EM structure of the delta1-40 CorM filament from cyanobacterium Anabaena sp. PCC 7120
Structure of glycosylphosphatidylinositol transamidase, state 3, unsharpened map
CryoEM structure of human MATa2 in complex with MAT2B isoform v1 at 2.6 A resolution
Cryo-EM structure of the Arabidopsis thaliana CAT4 transporter in the outward-open apo state (without synthetic nanobody)
In situ ribosome structure from environmental sample of Pseudo-nitzschia
Cryo-EM structure of Arabidopsis TIR-NLR WRR4A tetramer in complex with effector CCG40
CryoEM structure of human MATa2 in complex with MATBv2 at 2.6 A resolution
Hcp3-Tce1 complex from the Pseudomonas aeruginosa Type VI Secretion System
Evaluating the Volta Phase Plate for Improved Tomogram Alignment in Cryo-Electron Tomography: structure of 80S ribosome with VPP (full dataset)
Evaluating the Volta Phase Plate for Improved Tomogram Alignment in Cryo-Electron Tomography: structure of 70S ribosome with VPP (full dataset)
cryoEM structure of GluK2 LBD-TMD bound to glutamate in the shallow desensitized state
Structure of the SARS-CoV-2 S 6P trimer in complex with the cow antibody 99 Fab
Rabbit muscle aldolase cryo-EM reconstruction obtained from Glacios 3 with Selectris-X Falcon 4i detector
cryoEM structure of GluK2 LBD-TMD bound to BPAM344 and glutamate in the non-active state
cryoEM structure of GluK2 bound to BPAM344 and glutamate in the non-active state, composite map
SARS-CoV-2 Omicron BA.4 RBD in complex with Omi32 Fab and LC-Kappa VHH
Avian TRPM8 (Parus major) desensitized, fully-swapped, ligand-free structure resolved in cell vesicles using cryo-EM
SARS-CoV-2 Omicron BA.4 RBD in complex with Omi32 germline Fab and LC-Kappa VHH
Chimeric Escherichia coli 70S ribosome containing an evolved Vibrio cholerae 16S rRNA (VC-S4.4)
SARS-CoV-2 Omicron BA.1 RBD in complex with Omi32 germline Fab and LC-Kappa VHH
Chimeric Escherichia coli 70S ribosome containing an evolved 16S rRNA from Pseudomonas aeruginosa (PA-S3.3)
Escherichia coli 70S ribosome containing an evolved 16S rRNA (EC-S3.5)
The prefusion conformation of herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) mutant R131F
The deep-primed conformation of herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) mutant R131F
Cryo EM structure of glutamine synthetase from Brucella melitensis
The primed conformation of herpes simplex virus type 1 (HSV-1) glycoprotein B (gB) mutant R131F
Chimeric Escherichia coli 70S ribosome containing an evolved 16S rRNA from Pseudomonas aeruginosa (PA-ST)
Subtomogram average of nucleosome structure extracted from the HeLa cell nuclei
Subtomogram averaging of nucleosomes in reconstituted chromatin condensates
Heteromeric GluA1/A2-CNIH1 in the activated state, ligand binding domain (LBD)
CryoEM structure of mu-opioid receptor - Gi protein complex bound to FNZ- local map
Heteromeric GluA1/A2 in the activated state, transmembrane domain (TMD)
Heteromeric GluA1/A2-CNIH1 in the activated state, transmembrane domain (TMD)
Heteromeric GluA1/A2 in the inactive state, composite map of LBD-TMD
Heteromeric GluA1/A2 in the inactive state, transmembrane domain (TMD)
CryoEM structure of mu-opioid receptor - Gi protein complex bound to FNZ, Global Map
Heteromeric GluA1/A2 in the desensitized state, transmembrane domain (TMD)
Heteromeric GluA1/A2 in the activated state, consensus refinement of ATD-LBD-TMD
Heteromeric GluA1/A2 in the desensitized state, ligand binding domain (LBD)
Heteromeric GluA1/A2 in the inactive state, consensus refinement of LBD-TMD
Heteromeric GluA1/A2 in the inactive state, ligand binding domain (LBD)
