Composite Map Deposition Guide
Introduction
The deposition of a composite map entry set follows the recommendations laid out by the community in 2020 (https://doi.org/10.48550/arXiv.2311.17640). In accordance with these recommendations we require the composite map, all constituent maps (henceforth referred to as focused refinements), and the un-focused full structure (henceforth known as a consensus map) to be deposited as their own entries so that validation can be carried out for each of the deposited maps. In addition, the composite map entry must appropriately reference the focused refinements and consensus map. In this tutorial we will summarise the workflow to deposit a composite map set of entries in the most efficient manner possible.
In this tutorial we will use publicly available data EMDB: EMD-43299 and PDB: 8VK3.
Graphical Overview
To complete a deposition of a composite map set you will need several maps. These maps are described graphically below and EMD-IDs are included for an example composite map deposition set that can be found on the EMDB website.

Summary
Reminder: A composite map deposition must consist of separate depositions describing the composite map, consensus map, and focused map(s).
- Create a composite map deposition (Do not submit).
- Create focused refinement and consensus depositions (after completing composite map deposition). Pull the metadata from the composite map deposition.
- Associate the focused refinement and consensus depositions to the composite map deposition by filling the IDs in the “related entries” and submit.
Deposition Table
| Composite Map | Consensus Map | Focused Map(s) | |
|---|---|---|---|
| Primary Map |
Required |
Required |
Required |
| Half-maps |
Optional (If provided they must be composite half-maps)* |
Required |
Required |
| Entry Image |
Required |
Required |
Required |
| mmCIF file |
Optional (unless also depositing a model) |
Optional (unless also depositing a model) |
Optional (unless also depositing a model) |
| FSC Curve file |
Optional (If provided it should be calculated from the composite half-maps and described appropriately)** |
Optional |
Optional |
| Mask(s) |
Optional |
Optional |
Optional |
| Additional Map(s) |
Optional |
Optional |
Optional |
| Layer line file |
Not expected |
Not expected |
Not expected |
*If depositing half-maps as part of a composite-map deposition, only composite half-maps should be provided. Consensus and focused half-maps should be provided with the relevant, separate, depositions.
**EMDB recommends using the mean resolution of the focused maps as the resolution of the composite map
Step by Step
-
Start the composite map deposition
We recommend you start by creating the composite map deposition. This entry should contain all the metadata relevant to the other entries and we will be able to copy this across to those entries later. The deposition setup for this can be seen in Figure 1. Don’t forget to sign in with ORCID to enable easy access to all your depositions later on. In this example the model has been built into the composite map, therefore the composite map and model will be deposited together so that map-model validation can be carried out in this entry.

Figure 1: Setting up a composite map deposition.
Once the setup is complete and you have clicked ‘start deposition’ you should receive the details to login to the deposition via email and find it in your ORCID list of depositions if you were signed in with ORCID. The first step is to upload your files, an example of which can be seen in Figure 2, since this is a composite map deposition no half-maps are expected. Don’t forget that the mmCIF file format is also a metadata file format. All metadata provided in the uploaded mmCIF will automatically be used to fill the deposition interface. For users who wish to learn more about mmCIF files the mmCIF dictionary is available online (https://mmcif.wwpdb.org/) and example mmCIF files with EM metadata are available from the EMDB (e.g. https://www.ebi.ac.uk/emdb/EMD-43299?tab=links) under the Metadata section as a cif.gz download.

Figure 2: File upload page for a composite map entry.
After completing this section, the deposition interface will allow all metadata to be entered. Anything that was in the mmCIF file should already be in the deposition interface. Once all metadata sections are filled the entry should look similar to Figure 3.
DO NOT SUBMIT THE DEPOSITION YET!

Figure 3: a completed composite map deposition user-interface
We can now log out of this entry and start the deposition of the other entries.
2. Focused/Consensus map deposition
Now we are going to deposit the focused map(s) and consensus map. There should be one or more focused refinements and one consensus map deposited for every composite map deposited. In this example we will show you the deposition of a single focused refinement map, the method for depositing the others should be identical.
Once again we start by setting up the deposition (Figure 4). This time we will approach it as a regular map deposition (not composite). We have also already deposited coordinates with the composite map, as a result we will deposit the focused refinement(s) and consensus map without a coordinate model. If you have good reason to deposit portions of the model with the focused refinement(s) you are free to do so but where efficiency of deposition is concerned depositing the maps alone will be quicker.

Figure 4: Setting up a deposition for a focused/consensus map
As before, once the deposition is started you will get to the file upload screen. This time you can use the ‘based on a previous wwPDB deposition’ (Figure 5) option during the file upload process. This allows you to copy across various metadata from a previous deposition. Once the file upload is complete you should now see that, where possible, metadata has been transferred to the new deposition (Figure 6). This deposition can now be completed and submitted. Once submitted you will receive an EMD accession code which is needed for the next step.

Figure 5: Copying metadata from the composite map deposition

Figure 6: Metadata pulled from a previous deposition automatically fills relevant pages, in some cases already providing all required information (green tick).
3. Complete the composite map deposition
Now that you have completed all your focused refinement and consensus map depositions we can return to the composite map deposition and associate the new depositions to them. To do this we are going to go to the ‘Related entries’ page and fill the table out. The ‘content type’ drop-down menu will allow you to define the maps as focused or consensus. An example of this can be seen, including how it will be displayed on the EMDB website, in Figure 7. Once this is complete you are ready to submit the composite map deposition. If the composite map is accidentally submitted prematurely, or more entries are generated that you wish to be associated with the composite map after its submission, this can be corrected by contacting a wwPDB biocurator through the communication tab in OneDep.

Figure 7: Filling in the related entries for the composite map deposition.
Recommendation from EMDB: It is advised to use correlated yet distinct titles for entries related to a composite map.
Quick links
Recent Entries
(Show all)Structure of yeast Pol II complexed with a longer scaffold containing a cisplatin-induced inter-strand crosslink at the + 2 position.
Structure of yeast Pol II-Elf1 complex containing a cisplatin-ICL lesion at +7 position.
Structure of pre-translocation state of yeast Pol II complexed with a cisplatin-induced inter-strand crosslink at the +2 position.
Structure of post-translocation state of yeast Pol II complexed with a cisplatin-induced inter-strand crosslink at the +2 position.
Structure of backtracked yeast Pol II in complex with a cisplatin-induced inter-strand crosslink lesion at the +2 position.
Structure of yeast Pol II complexed with a longer scaffold containing a cisplatin-induced inter-strand crosslink lesion at the +5 position.
Structure of yeast Pol II in complex with a longer control scaffold lacking cisplatin-ICL lesion.
Structure of yeast Pol II in complex with an oxaliplatin-ICL lesion at +7 position.
Structure of yeast Pol II in complex with an oxaliplatin-ICL lesion at +2 position.
Structure of yeast post-translocation state Pol II in complex with a cisplatin-ICL lesion at +2 position in the second ICL DNA sequence.
Structure of yeast pre-translocation state Pol II in complex with a cisplatin-ICL lesion at +2 position in the second ICL DNA sequence.
HIV-1 Gag (CASP1NCSP2p6) assembled with core encapsidation signal - tomography map
HIV-1 Gag (CASP1NCSP2p6) assembled with dimerization signal - tomography map
The complex of A1AT-NHK with the ERAD misfolded glycoprotein checkpoint complex from Chaetomium thermophilum (EDEM:PDI heterodimer).
HIV-1 Gag (CASP1NCSP2p6) assembled with core encapsidation signal - C6 symmetry
HIV-1 Gag (CASP1NCSP2p6) assembled with core encapsidation signal - C1 symmetry
Apoferritin with crossed laser phase plate (xLPP), xLPP-off, paired dataset
Apoferritin with crossed laser phase plate (xLPP), xLPP-on, paired dataset
Evaluating the Volta Phase Plate for Improved Tomogram Alignment in Cryo-Electron Tomography: structure of PP7 virus-like-particle without VPP (full dataset)
Evaluating the Volta Phase Plate for Improved Tomogram Alignment in Cryo-Electron Tomography: structure of PP7 virus-like-particle with VPP (full dataset)
Structure of the kinase and central lobes of human CDK8 kinase module
Cryo-EM structure of the bacteriophage N4 virion RNA polymerase (closed plug state)
Cryo-EM structure of the bacteriophage N4 virion RNA polymerase (open plug state)
Cryo-EM structure of the bacteriophage N4 virion RNA polymerase (transcription initiation complex)
Babesia divergens ribosome structure by single-particle cryo-EM (3D class3, E-site tRNA)
Locally Refined Cryo-EM map of 2G12 IgG BCR receptor lacking Fab region view
Cryo-EM structure of the type III-D2 CRISPR-Cas effector complex bound to a cognate target RNA in the pre-cleavage state
Cryo-EM structure of the type III-D2 CRISPR-Cas effector complex bound to a cognate target RNA in the post-cleavage state
Cryo-EM structure of the type III-D2 CRISPR-Cas effector complex bound to a cognate target RNA in the pre-cleavage state
Cryo-EM structure of the type III-D2 CRISPR-Cas effector complex bound to a cognate target RNA in the post-cleavage state
Cryo-EM structure of the type III-D2 CRISPR-Cas effector complex bound to a non-cognate target RNA in the pre-cleavage state
Cryo-EM structure of the type III-D2 CRISPR-Cas effector complex bound to a non-cognate target RNA in the pre-cleavage state
Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (inactive state) (CASP target)
Eukaryotic translation initiation factor 2-B in its apo form (inactive-state) (CASP target)
Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (active-like-state) (CASP target)
Eukaryotic translation initiation factor 2-B in its apo form (active-state) (CASP target)
Eukaryotic translation initiation factor 2-B (eIF2B) bound to the viral effector AcP10
Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (active-like-state) asymmetrically bound to the viral effector AcP10 (CASP target)
Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta subunit (active-like-state) bound to the viral effector AcP10 (CASP target)
2.3 angstrom cryoEM map of endogenous nucleosome core particle in nuclear lysate
Cryo-EM structure of human Tom70 in complex with Hsp90 C-terminal EEVD peptide
Subtomogram average of septal junctions from Nostoc PCC7120 FraD-TM
Echovirus 18 particle missing three pentamers in situ, symmetrized reconstruction (C3)
Cryo-EM structure of Gephyrin in complex with Darpin 27F3, revealing linker-E domain interactions
Subtomogram average of septal junctions from Nostoc PCC7120 wild type
Cryo-EM structure of Gephyrin E domain in complex with Darpin 27F3
Cryo-electron tomogram of septal region from Nostoc PCC7120 FraD-TM
Cryo-electron tomogram of septal region from Nostoc PCC7120 FraD-TM
Cryo-electron tomogram of septal region from Nostoc PCC7120 wild type
In situ chromatosome structure from primary human T cells (C2 symmetry applied)
Cryo-EM structure of human apoferritin at 1.81 Angstrom resolution(using CR-BIS data collection on Falcon4).
Cryo-EM structure of human apoferritin at 1.79 Angstrom resolution(using BIS data collection on Falcon4).
In situ subtomogram average of 80S ribosome (local refined with LSU mask)
Cryo-EM structure of human apoferritin at 1.65 Angstrom resolution(using BIS data collection on Falcon4i).
Cryo-EM structure of human apoferritin at 1.64 Angstrom resolution(using CR-BIS data collection on Falcon4i).
Cryo-EM structure of human apoferritin at 2.05 Angstrom resolution(using CR-BIS data collection on K3).
Cryo-EM structure of human apoferritin at 2.05 Angstrom resolution(using BIS data collection on K3).
Subtomogram average structure of human apoferritin at 1.98 Angstrom resolution(using CR-BIS data collection on Falcon4i).
Subtomogram average structure of human apoferritin at 2.24 Angstrom resolution(using CR-BIS data collection on Falcon4).
Subtomogram average structure of human apoferritin at 2.01 Angstrom resolution(using BIS data collection on Falcon4i).
Subtomogram average structure of human apoferritin at 2.28 Angstrom resolution(using BIS data collection on K3).
Subtomogram average structure of human apoferritin at 2.34 Angstrom resolution(using BIS data collection on Falcon4).
Cryo-EM structure of heteromeric Kir4.1/5.1 potassium channel in complex with Ehop-016
Subtomogram average structure of human apoferritin at 2.21 Angstrom resolution(using CR-BIS data collection on K3).
C3 map of the filament formed by the grappling-hook like protein A from L. aerophila
Cryo-EM structure of TRP melastatin channel in the intermediate 2 state
Structure of a membrane-bound inositol phosphorylceramide synthase and Aureobasidin A complex
C1 map of the filament formed by the grappling-hook like protein A from L. aerophila
In situ chromatosome structure from primary human T cells (C1 symmetry applied)
Cryo-EM structure of TRP melastatin channel in the intermediate 1 state
Cryo-EM Structure of Parabacteroide phage PD491P1 head-to-tail interface
Cryo-EM structure of the tail tip region of Parabacteroide phage PD491P1 (imposed with C3 symmetry)
Structure of the Choline Transporter BetT under Acidic Conditions
Cryo-EM structure of the tail tip region of Parabacteroide phage PD491P1 (imposed with C6 symmetry)
Dark-state structure of human medium-wave-sensitive cone opsin (OPN1MW)
Pre-active dark-state structure of human short-wave-sensitive opsin (OPN1SW)
Dark-state structure of human short-wave-sensitive opsin (OPN1SW)
Cryo-EM structure of the human UAP56-RNA - SAC3D1-PCID2-SEM1 complex
CryoEM structure of human 20S proteasome in complex with proteasome inhibitor CP-17
Cryo-EM structure of the human UAP56-RNA - LENG8-PCID2-SEM1 complex
Cryo-EM structure of the human UAP56 NTD - LENG8-PCID2-SEM1 complex
Cryo EM structure of hemagglutinin from Puerto Rico/8/1934 (H1N1) in complex with a single domain antibody
Cryo EM structure of hemagglutinin from Puerto Rico/8/1934-New York/55/2004 (H3N2) in complex with a single domain antibody
Sheathed flagellar motor structure with C1 symmetry in Vibrio cholerae
Bacteriophage 812 prohead II with the complete set of minor capsid proteins
C1 symmetry cryoEM structure of the soluble-WRAPed membranous portion of MspA (Mycobacterium smegmatis porin), dimerized along the native interface.
Escherichia coli transcription-translation loosely coupled complex (TTC-LC^walked) containing mRNA with a 39 nt long spacer, NusG, NusA, and fMet-tRNAs in E-site and P-site - Map 1a
Bacteriophage 812 prohead II with minor capsid proteins with partial occupancy
Mitochondrial Creatine Kinase in complex with uncompetitive inhibitor uci
Local refinement of bottom five actins for One Lmod2 at the pointed end of F-actin
Local refinement of Lmod2 and the two terminal pointed end actins for One Lmod2 at the pointed end of F-actin
Consensus map for Two Lmod2s and incoming actin at the pointed end of F-actin
Local refinement of both Lmod2s, incoming actin, and the two terminal pointed end actins for Two Lmod2s and incoming actin at the pointed end of F-actin
Local refinement of the bottom five actins for Two Lmod2s and incoming actin at the pointed end of F-actin
SARS-CoV-2 RNA-dependent RNA polymerase in complex with 4'-FlA nucleotide analogue
Cryo-EM map of Ascl1-E12a in complex with NRCAM nucleosome without scFv
CryoEM structure of AdhE spirosome from Clostridium thermocellum uncovered by visual proteomics.
Cryo-electron microscopy structure of PfRIPR bound to monoclonal antibodies RP.093, RP.073 and RP.063
Cryo-electron microscopy structure of PfRIPR bound to monoclonal antibodies RP.047, RP.057 and RP.035
Cryo-electron microscopy structure of PfRIPR bound to monoclonal antibodies RP.092 and RP.052
Babesia divergens ribosome structure by single-particle cryo-EM (3D class1, A-, P-, and E-site tRNAs and mRNA)
Electron tomogram of the postmitotic nuclear envelope following acute Nup62 depletion
cryo-EM map of CH31 IgM BCR receptor representing immunoglobulin ectodomain, population 2
cryo-EM map of CH31 IgM BCR receptor representing immunoglobulin ectodomain, population-1
Cryo-EM map of CH31 IgM BCR receptor representing immunoglobulin ectodomain, population 3
In situ cryo-ET analysis of mitochondria and autophagosome contact in tauP301S Tg mouse cortical neurons
In situ cryo-ET analysis of mitochondria and autophagosome contact in tauP301S Tg mouse cortical neurons Supplementary 1
In situ cryo-ET analysis of mitochondria and autophagosome contact in tauP301S Tg mouse cortical neurons Supplementary 2
Transport and inhibition mechanisms of human glycine transporter 2
Transport and inhibition mechanisms of human glycine transporter 2
Structure of human Trpm4 in native lipid vesicles at 8 degrees celsius
Cryo-EM structure of macaque red cone pigment with Q114N mutation
Cryo-EM structure of macaque green cone pigment with Q114N mutation
Averaged protofilament of Heimdallarchaeales alpha/beta tubulin microtubule with a single seam
Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 WT) from Chaetomium thermophilum, state Rrp12-A2
Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 WT) from Chaetomium thermophilum, state Tsr1-1
Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 Mut) from Chaetomium thermophilum, state Rrp12-A1**
Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 WT) from Chaetomium thermophilum, state Tsr1-2
Cryo-EM structure of the 90S pre-ribosome (Enp1-Rrp12 WT) from Chaetomium thermophilum, state A
Cryo-EM structure of the 90S pre-ribosome (Enp1-Rrp12 WT) from Chaetomium thermophilum, state B1
Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 WT) from Chaetomium thermophilum, state Rrp12-A1
Cryo-EM structure of the 90S pre-ribosome (Enp1-Rrp12 Mut) from Chaetomium thermophilum, state B1*
Cryo-EM structure of the 90S pre-ribosome (Enp1-Rrp12 Mut) from Chaetomium thermophilum, state a
Cryo-EM structure of the 90S pre-ribosome (Enp1-Rrp12 Mut) from Chaetomium thermophilum, state B1
Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 Mut) from Chaetomium thermophilum, state Tsr1-1*
Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 Mut ) from Chaetomium thermophilum, state Rio2-C*
Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 WT) from Chaetomium thermophilum, state Tsr1-3
Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 Mut) from Chaetomium thermophilum, state Rrp12-A1*
Cryo-EM structure of the pre-40S ribosome (Enp1-Rrp12 WT) from Chaetomium thermophilum, state Rio2-C
Consensus map for Babesia divergens ribosome structure by single-particle cryo-EM (3D class1, A-, P-, and E-site tRNAs and mRNA)
Multi-body SSU body map for Babesia divergens ribosome structure by single-particle cryo-EM (3D class1, A-, P-, and E-site tRNAs and mRNA)
Multi-body LSU map for Babesia divergens ribosome structure by single-particle cryo-EM (3D class1, A-, P-, and E-site tRNAs and mRNA)
Multi-body SSU head map for Babesia divergens ribosome structure by single-particle cryo-EM (3D class1, A-, P-, and E-site tRNAs and mRNA)
Consensus map for Babesia divergens ribosome structure by single-particle cryo-EM (3D class3, E-site tRNA)
Cryo-EM local map of 2 VRC35 Fabs bound to HIV-1 BG505 DS-SOSIP.664 Env trimer
Multi-body LSU map for Babesia divergens ribosome structure by single-particle cryo-EM (3D class3, E-site tRNA)
Cryo-EM local map of 4 VRC35 Fabs bound to HIV-1 BG505 DS-SOSIP.664 Env trimer
Multi-body SSU head map for Babesia divergens ribosome structure by single-particle cryo-EM (3D class3, E-site tRNA)
Multi-body SSU body map for Babesia divergens ribosome structure by single-particle cryo-EM (3D class3, E-site tRNA)
Open Mtb-EC: Cryo-EM structure of Mtb RNAP elongation complex (substrate loading mimic) with an open active site (open TL and RH-FL)
SemiClosed Mtb-EC: Cryo-EM structure of Mtb RNAP elongation complex (substrate loading mimic) with a semiclosed active site (closed TL, open RH-FL)
CBR9379 bound Open1 Eco-ePEC: Cryo-EM structure of Eco RNAP his-elemental paused elongation complex with an open active site (open TL, SI3 and RH-FL)
AAP-SO2 bound Open Mtb-EC: Cryo-EM structure of Mtb RNAP elongation complex (substrate loading mimic) with an open active site (open TL and RH-FL)
Closed Mtb-EC: Cryo-EM structure of Mtb RNAP elongation complex (substrate loading mimic) with a closed active site (closed TL and RH-FL)
CBR9379 bound Open2 Eco-ePEC: Cryo-EM structure of Eco RNAP his-elemental paused elongation complex with an open active site (open TL, SI3 and RH-FL)
SemiClosed Eco-ePEC: Cryo-EM structure of Eco RNAP his-elemental paused elongation complex with a semi-closed active site (closed TL and SI3, open RH-FL)
Structure of yeast Pol II in complex with a cisplatin-induced inter-strand crosslink lesion at the +7 position.
Structure of mammalian RNA polymerase II stalled by a cisplatin-induced inter-strand crosslink lesion at the +2 position.
Structure of yeast Pol II in complex with a short control scaffold lacking cisplatin-ICL lesion.
Structure of yeast Pol II complexed with a longer scaffold containing a cisplatin-induced inter-strand crosslink at the + 3 position.
Structure of yeast Pol II in complex with a longer scaffold containing a cisplatin-ICL lesion at +7 position.
