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
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Cryo-EM structure of the inward-facing apo NhaA with flexible N-terminus at pH 6.3
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Cryo-EM structure of the inward-facing apo NhaA in the plugged state at pH 6.3
Cryo-EM structure of the inward-facing apo NhaA in the plugged state at pH 8.5
Structure of Crimean Congo hemorrhagic fever virus (CCHFV) L protein.
Cryo-EM structure of the inward-facing apo NhaA in the unplugged state at pH 5.5
Cryo-EM structure of the inward-facing apo NhaA in the unplugged state at pH 7.5
Cryo-EM structure of the consensus inward-facing apo NhaA dimer at pH 7.5
Cryo-EM structure of the inward-facing apo NhaA in the plugged state at pH 7.5
Cryo-EM structure of the inward-facing apo NhaA in the unplugged state at pH 6.3
Cryo-EM structure of the inward-facing apo NhaA in the open-funnel state at pH 8.5
Cryo-EM structure of the inward-facing apo NhaA in the unplugged state at pH 8.5
Cryo-EM structure of the inward-facing apo NhaA with flexible N-terminus at pH 8.5
PSI complex of A.thaliana isolated using DOC based Clear-Native-PAGE method
Tomogram of natural silk fibroin extracted from posterior silk glands
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Cryo-EM structure of a triangular-prism protein-DNA complex (D17-6-2t-10a/10b-T)
Cryo-EM structure of Chlamydomonas reinhardtii chloroplast F1Fo-ATP synthase
Cryo-EM structure of the inward-facing apo NhaA in the plugged state at pH 5.5
Cryo-EM structure of the inward-facing apo NhaA with flexible N-terminus at pH 5.5
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Focused refinement of turnover filament interface of glutamine synthetase
Naked mole-rat 80S ribosome in post-translocation non-rotated state
Naked mole-rat 80S ribosome in pre-translocation rotated hybrid state
Thermotoga maritima threonylcarbamoyl transfer complex (TsaB2D) in complex with Escherichia coli tRNA(THR)
Cryo-EM structure of NapA, the periplasmic nitrate reductase from Campylobacter jejuni
Thermotoga maritima threonylcarbamoyl transfer complex (TsaB2D) in complex with Thermotoga maritima tRNA(LYS)
Rabbit ribosomal 80S elongation complex with eEF2, partial P site Ala-tRNA, E site Ala-tRNA on NediV ORF
NediV IRES in complex with Rabbit 80S ribosome with eEF2 and P site Ala-tRNA
Rabbit ribosomal 80S elongation complex with eEF1A, A*/T Ala-tRNA, P site Ala-tRNA, E site Ala-tRNA on NediV ORF
PDX in Cell-Free Lysate Treated with Benzonase and Reverse-His purification
Artemia ferritin cell-free expression with reverse his purification and 1MDa MWCO Filtration
NediV IRES in complex with Rabbit 80S ribosome with A site Ala-tRNA
Structure of human Fab HB31 in complex with influenza H1N1 A/Solomon Island/3/2006 hemagglutinin
Structure of human Fab HB34 in complex with influenza H1N1 A/Solomon Island/3/2006 hemagglutinin
Structure of human Fab HB315 in complex with influenza H1N1 A/Solomon Island/3/2006 hemagglutinin
Open-AHD loperamide-mu opioid receptor-Gi GDP complex (constant GDP) - Locally refined Gi map
Artemia ferritin cell-free expressed and filtered using 300 kDa MWCO
Open-AHD naloxone-mu opioid receptor-Gi GDP complex (constant GDP) - Consensus map
Engaged-state naloxone-mu opioid receptor-Gi GDPbS complex (rebound) - Consensus map
Latent-state naloxone-mu opioid receptor-Gi GDP complex (constant GDP) - Consensus map
Cryo-EM Structure of Human C3 Pro-Convertase bound to the Compstatin Analog Cp60, TED Conformation 2
Engaged-state naloxone-mu opioid receptor-Gi GDP complex (constant GDP) - Consensus map
Artemia ferritin cell-free expression with reverse his purification and 1MDa filtration
Cryo-EM Structure of Human C3 Pro-Convertase bound to the Compstatin Analog Cp60, TED Conformation 1
The cryo-EM structure of ATRX in complex with the nucleosome in the ADP.BeFx-bound state (composite)
CryoEM structure of transcribing RNA polymerase II elongation complex with ATP and Elf1_3D classification map containing the complete nucleic acid scaffold
CryoEM structure of transcribing RNA polymerase II elongation complex with ATP and Elf1
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TnsC-focused cryo-EM volume of the PseCascade-TniQ-TnsC complex bound to TnsB-hook motifs
Consensus cryo-EM volume of the PseCascade-TniQ-TnsC-TnsAB holocomplex
Cryo-EM structure of the PseCascade-TniQ-TnsC complex bound to PseTnsB-hook motifs
TnsAB-focused cryo-EM volume of the PseCascade-TniQ-TnsC-TnsAB holocomplex
Cascade-TniQ-TnsC-focused cryo-EM volume of the PseCascade-TniQ-TnsC-TnsAB holocomplex
Siphohage OE33PA upon binding to its Gram+ host cell surface (view 2)
Siphohage OE33PA upon binding to its Gram+ host cell surface (view 1)
Siphohage OE33PA upon binding to its Gram+ host cell surface (view 4)
Siphohage OE33PA upon binding to its Gram+ host cell surface (view 3)
Siphohage OE33PA upon binding to its Gram+ host cell surface (view 5)
Siphohage OE33PA upon binding to its Gram+ host cell surface (view 6)
DNA in the capsid-tail connector of the phage OE33PA (classification focused on the adaptor-stopper region)
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DNA in the capsid-tail connector of the phage OE33PA (classification focused on the capsid-portal junction)
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adhesion device (C3 symmetrized reconstruction) of the phage OE33PA
C6 symmetrized reconstruction of the adhesion device of the phage OE33PA
RBP trimer bound to a monomer of the distal tail protein of the phage OE33PA
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Conformational variability of the phage OE33PA adhesion device (State 2)
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Cryo-EM structure of monomeric Cu/Zn-superoxide dismutase from dog (Canis familiaris) complexed with 19A9 triabody in the open conformation
Cryo-EM structure of Tundra swan ACE2 complexed with SARS-CoV-2 RBD
Cryo-EM structure of Black swan ACE2 complexed with SARS-CoV-2 RBD
Structure of human proteasome ATPase-CP intermediate assembles with 90min rapaprotin addition
Structure of human proteasome ATPase-CP intermediate assembles with 90min rapaprotin addition
Structure of human proteasome ATPase-CP intermediate assembles with 15min rapaprotin addition
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cryoEM structure of hexametric HtrA from Borrelia burgdorferi with bound peptides in the active sites
BRCA1-A complex bound to K63-polyUbATA - open form double State P
BRCA1-A complex: Ubiquitin bound to BRE at the wrist site (focused 3D class)
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Pr-Pfr heterodimer state of Stigmatella aurantiaca bacteriophytochrome 2
Pr-pr homodimer state of Stigmatella aurantiaca bacteriophytochrome 2
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Cryo-EM structure of human TRPM4 channel in the warm conformation in complex with calcium and TPPO at 37 degrees Celsius (monomeric TMD-focused map with best-resolved TPPO density)
Human telomerase catalytic core with shelterin protein TPP1, dGpNHpp and DNA primer ending in TTAG
Human telomerase catalytic core with shelterin protein TPP1, BIBR1532 and DNA primer ending in AGGG
Human telomerase catalytic core with shelterin protein TPP1, BIBR1532 and DNA primer ending in TTAG
Class III (T1D0) of Human telomerase catalytic core with shelterin protein TPP1, BIBR1532, dGpNHpp and DNA primer ending in TTAG
Class I (T1D0+) of Human telomerase catalytic core with shelterin protein TPP1, BIBR1532, dGpNHpp and DNA primer ending in TTAG
Class II ("T0D0") of Human telomerase catalytic core with shelterin protein TPP1, BIBR1532, dGpNHpp and DNA primer ending in TTAG
Human telomerase catalytic core with shelterin protein TPP1 and DNA primer ending in TTAG
Human telomerase catalytic core with shelterin protein TPP1, BIBR1532, dTpNHpp and DNA primer ending in AGGG
Human telomerase catalytic core with shelterin protein TPP1, dTpNHpp and DNA primer ending in AGGG
Cryo-EM structure of the DDB1deltaB-CRBN-Pomalidomide complex bound to IKZF1(ZF1-ZF2-Helix)
Cryo-EM structure of the DDB1deltaB-CRBN-Pomalidomide complex bound to SALL4(ZF1-ZF2-Helix)
Cryo-EM structure of the DDB1deltaB-CRBN-ALV2 complex bound to HELIOS
Cryo-EM structure of SARS-CoV-2 BA.3.2.1 spike with K852A mutation, flexible conformation
Cryo-EM structure of SARS-CoV-2 BA.3.2.1 spike with N529Q mutation, open conformation
Cryo-EM structure of SARS-CoV-2 BA.3.2.1 spike with N529Q mutation, flexible conformation
Composite Map of the Macrocystis pyrifera Photosystem I Supercomplex
Local refinement of RBDA, RBDC, and NTDB of SARS-CoV-2 BA.3.2.1 spike with K852A mutation, closed conformation
Local refinement of the RBD and NTD in the closed BA.3.2.1 spike with N529Q mutant
Local refinement of hACE2/SARS-CoV-2 LP.8.1 spike, conformation 1
Cryo-EM structure of SARS-CoV-2 BA.3.2.1 Spike with K852A mutation, closed conformation
Cryo-EM structure of SARS-CoV-2 BA.3.2.1 spike with K852A mutation, open conformation
Cryo-EM structure of SecM-arrested 70S ribosome with YheS, local-masked refined map on LSU.
Cryo-EM structure of SecM-arrested 70S ribosome with YheS, the overall refined map
Cryo-EM structure of SecM-arrested 70S ribosome with YheS, local-masked refined map on the SSU body.
Cryo-EM structure of SecM-arrested 70S ribosome with YheS, local-masked refined map on the SSU head.
Cryo-EM structure of SecM-arrested 70S ribosome with YheS, local-masked refined map on YheS and L1 stalk.
Cryo-EM structure of EB1002-bound neurokinin 2 receptor (NK2R) in complex with miniGs/q70
Cryo-EM structure of neurokinin A (NKA)-bound neurokinin 2 receptor (NK2R) in complex with miniGs/q70
Cryo-EM structure of EB1001-bound neurokinin 2 receptor (NK2R) in complex with miniGs/q70
Cryo-EM structure of Peptide 336 (P336)-bound neurokinin 2 receptor (NK2R) in complex with miniGs/q70
Cryo-EM structure of Peptide 383 (P383)-bound neurokinin 2 receptor (NK2R) in complex with miniGs/q70
Solution structure of Clostridioides difficile CspA protein in complex with CspC and Taurocholate, determined by CryoEM
Solution structure of Clostridioides difficile CspB protein determined by CryoEM
Echovirus 18 particle missing one pentamer in situ, asymmetric reconstruction
Echovirus 18 particle missing three pentamers in situ, asymmetric reconstruction
Local refinement of BA.3.2 spike (3-RBD-down), RBD-A, RBD-C and NTD-B
Echovirus 18 particle missing two pentamers in situ, asymmetric reconstruction
Echovirus 18 particle missing one pentamer in situ, symmetrized reconstruction (C5)
Solution structure of Clostridioides difficile CspB oligomer determined by CryoEM
Echovirus 18 particle missing two pentamers in situ, symmetrized reconstruction (C2)
P1a-state of wild type human mitochondrial LONP1 protease with bound substrate protein, ADP and aluminum fluoride
Local refinement of hACE2/SARS-CoV-2 BA.3.2.1 spike, conformation 1
Cryo-EM structure of Aspergillus fumigatus ErdS dimer with tRNA(Asp) acceptor stem in an intermediate position toward the ATT active site
Cryo-EM structure of Aspergillus fumigatus ErdS dimer with tRNA(Asp) acceptor stem docked at the AspRS active site
Local refinement of the receptor in the cryo-EM map of the Gq-coupled LPAR5 in complex with LPA
Local refinement of the G protein and scFv16 in the cryo-EM map of the Gq-coupled LPAR5 in complex with LPA
