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)Pentamer Msp1 from S.cerevisiae (with a catalytic dead mutation) in complex with an unknown peptide substrate state2
STRUCTURE OF UNSTACKED C2S2-TYPE PSII-LHCII SUPERCOMPLEX FROM PISUM SATIVUM
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C12 reconstruction of the thermophilic bacteriophage P74-26 Collar-less Neck
C1 reconstruction of the thermophilic bacteriophage P74-26 Portal and Portal Vertex
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Asymmetric reconstruction of filled phage capsids lacking neck and tail
Motor domains of phi-like human dynein-1 bound to dynactin-p150glued and LIS1
Motor domain of human dynein-1 in pre-power stroke bound to dynactin-p150glued-CC1B and LIS1
12.7-Angstrom resolution structure of bacteriophage Sf6 in the C1 symmetry by cryo-electron tomography and sub-tomogram averaging with 538 particles reveal the tail appendage
Asymmetric reconstruction of filled phage capsids with broken tails
Mitochondrial Creatine Kinase in complex with ADP and uncompetitive inhibitor uci
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Composite reconstruction of the thermophilic bacteriophage P74-26 Neck and Portal Vertex
Dynactin and dynein-1 tail region of dynein-dynactin complex on microtubule in the presence of LIS1
Cryo-EM structure of F-box helicase 1 (FBH1) bound to an SCF ubiquitin ligase complex and a 3-way DNA fork (head structure)
9.1-Angstrom resolution structure of the portal protein core of bacteriophage Sf6 by cryo-electron tomography and sub-tomogram averaging with 538 particles
Human Oct4 bound to nucleosome reconstituted with human histones and 182 bp human LIN28B sequence
Cryo-EM structure of F-box helicase 1 (FBH1) bound to an SCF ubiquitin ligase complex and a 3-way DNA fork (body structure)
Cryo-EM structure of F-box helicase 1 (FBH1) bound to an SCF ubiquitin ligase complex and a 3-way DNA fork (consensus structure)
Cryo-EM structure of F-box helicase 1 (FBH1) bound to an SCF ubiquitin ligase complex and a 3-way DNA fork (substrate structure)
Focused refinement map of the human M4 muscarinic acetylcholine receptor bound to the bitopic agonist C110
Human M4 muscarinic acetylcholine receptor Gi1 complex (mini-Gsi chimera) bound to the bitopic agonist C110
cryo-ET subtomogram-averaged structure of mouse heavy-chain apoferritin resolved at 2.71 Angstroms
Human TRPM4 ion channel in MAASTY copolymer lipid nanodisc in a calcium-bound state
Open state of A8 gpJ 713 central tail fiber with OmpC G17 from E. coli EDL933
Methanosarcina acetivorans 70S ribosome in complex with SriA and SriB composite map
Methanosarcina acetivorans 70S ribosome in complex with SriD composite map
Methanosarcina acetivorans 70S ribosome in complex with SriC and SriD 30S focused refinement
Methanosarcina acetivorans 70S ribosome in complex with SriC and SriD 30S head focused refinement
Methanosarcina acetivorans 70S ribosome in complex with SriC and SriD consensus map
Methanosarcina acetivorans 70S ribosome in complex with SriA and SriB consensus map
Methanosarcina acetivorans 70S ribosome in complex with SriA and SriB 50S focused refinement
Methanosarcina acetivorans 70S ribosome in complex with SriD 30S focused refinement
Methanosarcina acetivorans 70S ribosome in complex with SriC and SriD 50S focused refinement
Methanosarcina acetivorans 70S ribosome in complex with SriA and SriB 30S focused refinement
Methanosarcina acetivorans 70S ribosome in complex with SriD consensus map
Methanosarcina acetivorans 70S ribosome in complex with SriD 50S focused refinement
Methanosarcina acetivorans 70S ribosome in complex with SriA and SriB 30S head focused refinement
Methanosarcina acetivorans 70S ribosome in complex with SriC and SriD composite map
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Consensus olfactory receptor bmOR6A2 in complex with mini-Golf trimeric protein
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Asymmetrically gated state sheep connexin-46/50 in DMPC nanodiscs at low pH
Destabilized open state sheep connexin-46/50 in DMPC nanodiscs at low pH
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Cryo-EM structure of SARS-CoV-2 JN.1 spike glycoprotein in complex with F61R2-780 Fab
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Local refinement of stacked like DDB1-DDA1-DET1-Ube2e2-COP1 complex (layer 2)
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Structure of E.coli ribosome with nascent chain at linker length of 31 amino acids, with mRNA, P-site and A-site tRNAs
Local Refinement of human M4 muscarinic acetylcholine receptor G protein complex bound to selective PAM Emraclidine
Composite map: Ternary complex of the human 20S proteasome in complex with Importin-9 and two homodimers of Akirin-2
Structural characterisation of chromatin remodelling intermediates supports linker DNA dependent product inhibition as a mechanism for nucleosome spacing.
Ternary complex of the human 20S proteasome in complex with Importin-9 and two homodimers of Akirin-2 - focussed refinement on Importin-9 and Akirin-2
Binary complex of human Importin-9 with one homodimer of Akirin-2
Structural characterisation of chromatin remodelling intermediates supports linker DNA dependent product inhibition as a mechanism for nucleosome spacing.
Ternary complex of the human 20S proteasome in complex with Importin-9 and two homodimers of Akirin-2 - focussed refinement on the alpha subunits, Ipo-9 and Ak2
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Cryo-EM structure of the catalytic core of human telomerase at the initiation state of the repeat addition cycle
Cryo-EM structure of the catalytic core of human telomerase at the pre-termination state of the repeat addition cycle
Asymmetric hexameric MmpS4-MmpL4 complex from Mycobacterium tuberculosis with "short" coiled-coil domain
Symmetric hexameric MmpS4-MmpL4 complex from Mycobacterium tuberculosis
Asymmetric hexameric MmpS4-MmpL4 complex from Mycobacterium tuberculosis with "long" coiled-coil domain
6-fold-symmetric reconstruction focused on the middle part of the bacteriophage T4 tail
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Cryo-EM structure of SARS-CoV-2 nsp10-nsp14 (E191A) in complex with T20P14-S complex, tetrameric form
Cryo-EM structure of SARS-CoV-2 nsp10-nsp14 (E191A) in complex with T20P14-B complex, protomer A focused refinement
Cryo-EM structure of SARS-CoV-2 nsp10-nsp14 (E191A) in complex with T20P14-B complex, dimeric form
6-fold-symmetric reconstruction focused on the bacteriophage T4 baseplate
6-fold-symmetric reconstruction focused on the bacteriophage T4 neck region
Structure of the bacteriophage T4 portal-neck-tail connector complex
In situ cryo-electron tomogram of 4days WT nucleus (trimer close to NE)
Cryo-EM structure of human lipid phosphate phosphatase 1 complexed with PO4 in nanodiscs
Twenty-two polymer Msp1 from S.cerevisiae(with a catalytic dead mutation) in complex with an unknown peptide substrate
Sixteen polymer Msp1 from S.cerevisiae (with a catalytic dead mutation) in complex with an unknown peptide substrate
