Happy Holidays and New year from the EMDB! Please be advised that the EMDB team will be operating at reduced capacity between December 15th - January 12th. With this in mind we would ask that you be prepared for longer reply times through both our helpdesk system and the OneDep deposition system. well done on a productive 2025, wishing you all the best and we will see you in 2026!
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)Cryo-EM structure of SARS-CoV-2 KP.2 spike RBD in complex with ACE2
Yeast 80S with nascent chain in complex with Ssb1-ADP in the S2 state
Human pannexin 1 channel from combined 0, 10, 20, 30 mM ATP datasets
Cryo-EM reconstruction of PI3KC3-C2 in complex with Rubicon Middle Region of C terminus, focused map 2/2
Cryo-EM reconstruction of PI3KC3-C2 in complex with Rubicon Middle Region of C terminus, composite map
Cryo-EM reconstruction of PI3KC3-C2 in complex with Rubicon Middle Region of C terminus, focused map 1/2
Cryo-EM structure of human PI3KC3-C2 in complex with Rubicon Middle Region of C terminus
Co-transcriptional histone H3K36 methylation complex containing RNA polymerase II elongation complex, Set2, and the upstream nucleosome. (temp115, type A)
Co-transcriptional histone H3K36 methylation complex containing RNA polymerase II elongation complex, Set2, and the upstream nucleosome. (temp115, type B)
Co-transcriptional histone H3K36 methylation complex containing RNA polymerase II elongation complex, Set2, and the upstream nucleosome. (temp130, type B)
Co-transcriptional histone H3K36 methylation complex containing RNA polymerase II elongation complex, Set2, and the upstream nucleosome. (temp130, type A)
The complex structure of 0086-0043 and NET determined with Cryo-EM.
The complex structure of Y510-9709 and NET determined with Cryo-EM
Co-transcriptional histone H3K36 methylation complex containing RNA polymerase II elongation complex, Set2, and the upstream nucleosome. (temp115, FACT-hexamer)
consensus map of Neddylated CUL5-ARIH2-L3A2-1 bound to ASB9-EloB/C-CKB
Structure of the Complement classical and lectin pathway C3 convertase
Consensus Map of Neddylated CUL5 C-terminal region-RBX2-ARIH2~L3A2-1~Ub
Structure of the Complement classical and lectin pathway proconvertase, C4b2
Structure of the Complement classical and lectin pathway C3 convertase in complex with substrate C3
Focus refined map of Neddylated CUL5 C-terminal region-RBX2-ARIH2~L3A2-1~Ub
Cerebellar GluA2/4 NTD heterophilic tetramer interface (focused refinement)
GluA4 N-terminal domain bound to nanobody NB74 (focused refinement)
Structure of Neddylated CUL5 C-terminal region-RBX2-ARIH2~L3A2-1~Ub
Structure of the Complement classical and lectin pathway proconvertase, C4b2
Focus refined map of Neddylated CUL5-ARIH2-L3A2-1 bound to ASB9-EloB/C-CKB, focus refined on ARIH2-L3A2-1
Cryo-EM map of focus refined ASB9-Elob/C-CKB bound to Nedd8-CUL5-RBX2-ARIH2-L3A2-1
P116 from Mycoplasma pneumoniae in complex with mild growth suppressor monoclonal antibody
cryoEM structure of the B-chain of the human OGA-L Catalytic Dimer
cryoEM structure of the A-chain of the human OGA-L Catalytic Dimer
cryoEM structure of the human OGA-L Catalytic Dimer, extra A-chain density
Low-resolution electron density map of C. elegans PEZO-1 Isoform L
Structure-Guided Design of Picomolar-level Macrocyclic TRPC5 Channel Inhibitors with Antidepressant Activity
Structure of the wild-type ABCC2 in Arabidopsis thaliana in the apo state
Cryo-EM structure of amyloid peptide-silk block protein fibril, Type 2
Structure of ABCC2(E1404Q) in Arabidopsis thaliana in the apo state
Structure of ABCC2(E1404Q) in Arabidopsis thaliana in the DNP-GS bound state
Structure of ABCC2(E1404Q) monomer in Arabidopsis thaliana in the DNP-GS bound state
Structure of ABCC2(E1404Q) in Arabidopsis thaliana in the ATP bound state
Structure of the wild-type ABCC2 dimer in Arabidopsis thaliana in the apo state
Cryo-EM structure of renal amyloid fibril from an immunoglobulin light chain amyloidosis patient in polymorph B
Cryo-EM structure of renal amyloid fibril from an immunoglobulin light chain amyloidosis patient in polymorph A
Consensus map of KATP channel in complex with centipede toxin SpTx1
C. thermocellum UvrA in complex with unmodified DNA and AMPPNP (ATP-bound conformation 1)
C. thermocellum UvrA in complex with unmodified DNA and AMPPNP (ATP-bound conformation 2)
C. thermocellum UvrA in complex with unmodified DNA and AMPPNP (basal conformation)
C. thermocellum UvrA in complex with DNA with a fluorescein modification (basal conformation)
C. thermocellum UvrA in complex with DNA with a fluorescein modification and AMPPNP (ATP-bound conformation 1)
C. thermocellum UvrA in complex with DNA with an abasic site (basal conformation)
C. thermocellum UvrA in complex with DNA with an abasic site and AMPPNP (ATP-bound conformation 2)
C. thermocellum UvrA in complex with DNA with an abasic site and AMPPNP (ATP-bound conformation 1)
C. thermocellum UvrA in complex with DNA with a fluorescein modification and ADP (basal conformation)
C. thermocellum UvrA (K647A) in complex with DNA with a fluorescein modification (basal conformation)
C. thermocellum UvrA (K39A) in complex with DNA with a fluorescein modification and AMPPNP (basal conformation)
C. thermocellum UvrA-UvrB in complex with DNA with a fluorescein modification and AMPPNP (composite map)
a5b3 GABAAR bound to Etomidate, GABA, and Mb25 in a desensitized state in saposin nanodiscs
a5b3 GABAA Receptor bound to GABA and Mb25 in desensitized state in detergent micelles
a5b3 GABAA Receptor in 1 a5 to 4 b3 stoichiometry in desensitized state
a5b3 GABAAR bound to GABA and Mb25 in a desensitized state in saposin nanodiscs after long GABA treatment
Hexamer Msp1 from S.cerevisiae (with a catalytic dead mutation) in complex with an unknown peptide substrate
Core filament of the spirochete periplasmic flagella of Leptospira biflexa
core filament of the spirochete periplasmic flagella of Leptospira biflexa wild type
core filament of the spirochete periplasmic flagella of Leptospira biflexa deleted fcpB strain
Octamer Msp1 from S.cerevisiae(with a catalytic dead mutation) in complex with an unknown peptide substrate
core filament of the spirochete periplasmic flagella of Leptospira biflexa from the flaA2-complemented stain
Straight and symmetrical filament of the spirochete periplasmic flagella of Leptospira biflexa
core filament of the spirochete periplasmic flagella of Leptospira biflexa from the deleted fcpB_CL13 strain
Sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the deleted fcpB_CL13 strain
Straight and symmetrical filament of the spirochete periplasmic flagella of Leptospira biflexa deleted fcpB strain
Heptamer Msp1 from S.cerevisiae(with a catalytic dead mutation) in complex with an unknown peptide substrate
sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa wild type
sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the flaA2-complemented stain
Negative stain EM map of EBV glycoprotein gH/gL in complex with glycoprotein gp42 and FAB ATX-42-1.1 partially open conformation
Negative stain EM map of EBV glycoprotein gH/gL in complex with glycoprotein gp42 and FAB ATX-42-2 closed conformation
Negative stain EM map of EBV glycoprotein gH/gL in complex with glycoprotein gp42 and HLA-DR1 Beta chain
Negative Stain EM map of EBV glycoprotein gp350 in complex with ATX-350-2 FAB
Negative Stain EM map of EBV glycoprotein gp350 in complex with 72A1 FAB
Negative Stain EM map of EBV glycoprotein gp350 in complex with ATX-350-1 FAB
Negative Stain EM map of EBV glycoprotein gp350 in complex with ATX-350-1 FAB and 72A1 FAB
Structure of a LGR dimer from Caenorhabditis elegans in apo state
Negative stain EM map of EBV glycoprotein gH/gL in complex with glycoprotein gp42 and FAB ATX-42-2 Open conformation
Globular domain of monkeypox virus OPG153 (A28) in complex with antibodies 08E11 and 12I12
Globular domain of monkeypox virus OPG153 (A28) bound to antibody 02M12
Negative stain EM map of EBV glycoprotein gH/gL in complex with glycoprotein gp42 and FAB ATX-42-1.1 open conformation
Cryo-EM structure of MERS-CoV nsp10-nsp14 (E191A) in complex with T20P14-G RNA
Cryo-EM structure of MERS-CoV nsp10-nsp14 (E191A) in complex with T20P14-A RNA
Cryo-EM structure of MERS-CoV nsp10-nsp14 (E191A) in complex with T20P14-U RNA
Cryo-EM structure of MERS-CoV nsp10-nsp14 (E191A) in complex with T20P15 RNA, dimeric form
Cryo-EM structure of MERS-CoV nsp10-nsp14 (E191A) in complex with T20P15 RNA, monomeric form
In situ HHT and CHX treated human eEF1A-A/T-P-Z state 80S ribosome
Structure of E. Coli DNA protection during starvation protein (DPS) from single particle cryoEM
In situ human unrotated hibernating without CCDC124 state 80S ribosome
In situ human unrotated hibernating with CCDC124 state 80S ribosome
In situ human Hibernating class1 (rotate3) without E tRNA state 80S ribosome
In situ human Hibernating rotate3 with Z site tRNA state 80S ribosome
In situ human Hibernating rotate 3 with E-site tRNA state 80S ribosome
C. thermocellum UvrA-UvrB in complex with DNA with a fluorescein modification and AMPPNP: consensus map
C. thermocellum UvrA-UvrB in complex with DNA with a fluorescein modification and AMPPNP: focused map
Structure of the Chaetomium thermophilum Pmt4 homodimer (C2 symmetry)
Structure of the Chaetomium thermophilum Pmt4 homodimer (C1 symmetry)
Structure of human 1918 influenza A polymerase heterotrimer in complex with 1918 NEP.
Yeast 80S with nascent chain in complex with Ssb1-ADP in the S1 state
Structure of human 1918 influenza A polymerase heterotrimer in complex with WSN NEP.
structure of bundle-shaped PBS with both long rod and (ApcA2B3ApcD) trimer
Structure of the energy converting methyltransferase (Mtr) of Methanosarcina mazei in complex with a novel protein binder
Structure of the energy converting methyltransferase (Mtr) of Methanosarcina mazei in complex with a novel protein binder
Structure of the energy converting methyltransferase (Mtr) of Methanosarcina mazei in complex with a novel protein binder
Structure of the energy converting methyltransferase (Mtr) of Methanosarcina mazei in complex with a novel protein binder
Subtomogram averaging of HTLV-1 Gag capsid from immature particles
Microtubules in presence of Ndc80 and Ska, non-Ndc80 microtubule-bound molecules
Focused-Refinement Cryo-EM Map of the RAZR-ZFD Domain within the In Vitro Reconstituted RAZR.Gp77 Complex
Cryo-EM Structure of Gp77 within the In Vitro Reconstituted RAZR:GP77 Complex
Cryo-EM Map of the Copurified Ring-Activated Zinc-Finger RNase (RAZR, H154A) in Complex with Phage Protein Gp77
Cryo-EM map of the in vitro reconstituted RAZR:GP77 complex with AlphaFold-predicted models fitted into the density.
Cryo-EM structure of the dCas12f-gRNA-dsDNA complex (full R-Loop)
Cryo-EM structure of the dCas12f-gRNA-DNA complex (partial R-Loop)
Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome CDC73 local map J
Cryo-EM structure of active human green cone opsin in complex with chimeric G protein (miniGist)
Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome RPB5 local map I
Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome non-template DNA local map H
Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome CTR9+WDR61 local map K
Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome CTR9 TPR local map L
Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome PAF1+LEO1 local map M
Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome LEO1 C-terminus map N
Pol II-DSIF-SPT6-PAF1c-TFIIS-IWS1-ELOF1-LEDGF-nucleosome SPT6 local map O
Subtomogram average of influenza hemagglutinin (A/Puerto Rico/8/1934)
Mycobacterium smegmatis 70S ribosome with small molecule drug MK-7762
