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)Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state ED0.2
Focused map of CXCL10-CXCR3 (components of CXCL10-CXCR3-Gi-scFv16)
Focused map of CXCL11-CXCR3 (components of CXCL11-CXCR3-Gi-scFv16)
MvhAGD-focused map of the mobile arm under state 2 substate b of M. marburgensis
HdrBC-focused map of the mobile arm under state 2 substate b of M. marburgensis
Cryo-EM structure of plant resistance protein NRC2 dimer bound to nematode effector SPRYSEC-15
Focused map of the FmdF dimer unit of the Mvh-Hdr-Fmd complex of M. marburgensis
Focused map of the FmdABCFG(2) unit of the Mvh-Hdr-Fmd complex of M. marburgensis
Focused map of the FmdABCFG(1) unit of the Mvh-Hdr-Fmd complex of M. marburgensis
Focused map of the C-terminus of the MvhB subunit of the Mvh-Hdr-Fmd complex of M. marburgensis
Focused map of the MvhB subunit of the Mvh-Hdr-Fmd complex of M. marburgensis
HdrA-focused map of the mobile arm under state 2 substate b of M. marburgensis
Consensus map of the mobile arm under state 2 substate a of M. marburgensis
HdrA-focused map of the mobile arm under state 2 substate a of M. marburgensis
HdrBC-focused map of the mobile arm under state 1 substate b of M. marburgensis
HdrA-focused map of the mobile arm under state 1 substate a of M. marburgensis
MvhAGD-focused map of the mobile arm under state 1 substate b of M. marburgensis
Consensus map of the mobile arm under state 2 substate b of M. marburgensis
MvhAGD-focused map of the mobile arm under state 1 substate a of M. marburgensis
HdrA-focused map of the mobile arm under state 1 substate b of M. marburgensis
MvhAGD-focused map of the mobile arm under state 2 substate a of M. marburgensis
Consensus map of the mobile arm under state 1 substate b of M. marburgensis
HdrBC-focused map of the mobile arm under state 1 substate a of M. marburgensis
HdrBC-focused map of the mobile arm under state 2 substate a of M. marburgensis
Structure of the MvhAGD-HdrABC dimer of M. marburgensis under state 1 substate a (composite structure)
Consensus map of the mobile arm under state 1 substate a of M. marburgensis
Structure of the MvhAGD-HdrABC dimer of M. marburgensis under state 1 substate b (composite structure)
Structure of the MvhAGD-HdrABC dimer of M. marburgensis under state 2 substate a (composite structure)
Human vault protein - local refinement of the waist - committed conformation
Structure of the MvhAGD-HdrABC dimer of M. marburgensis under state 2 substate b (composite structure)
Structure of the Mvh-Hdr-Fmd complex of Methanothermobacter marburgensis (composite structure)
Consensus low resolution map of the flavin-bifurcating CO2-fixing Mvh-Hdr-Fmd supercomplex from Methanothermobacter marburgensis
Global map of six VRC35 Fabs and three MEDI8852 Fabs bound to influenza H3N2 Victoria 2011 hemaglutinin
Focused refinement of PP2Ac repeat 1 of the FBXO42-CCDC6-PP2Ac degradasome
Cryo-EM structure of human VCP/p97-T122P mutant bound to ATPgammaS
Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state
Cryo-EM structure of human VCP/p97-G156D mutant bound to ATPgammaS
Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state
Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state
Focussed refinement map of ATPase lobe 2 of human lymphoid-specific helicase HELLS
Structure of human lymphoid-specific helicase HELLS in its auto-inhibitory state
SthK closed state at low temperature, cAMP-bound in DOPC nanodiscs
Closed Eco-ePEC: Cryo-EM structure of Eco RNAP his-elemental paused elongation complex with a closed active site (closed TL, SI3 and RH-FL)
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)
CA-SP1 immature lattice assembled in vitro with inhibitor lenacapavir (dialyzed to 50nM)
Gag CA-SP1 immature lattice bound with Lenacapavir from enveloped virus like particles
eN49P7-FRv1-23 Fab in complex with BG505 MD39 SOSIP and RM20A3 Fab
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)
Open3 Eco-ePEC: Cryo-EM structure of Eco RNAP his-elemental paused elongation complex with an open active site (open TL, SI3 and RH-FL)
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 1-nt gapped DNA in state 2 conformer 1 with sharply bent DNA
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 1-nt gapped DNA in state 1 conformer 1 with flexibly bound DNA at the shoulder
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 1-nt gapped DNA in state 1 conformer 2 with flexibly bound DNA at the shoulder
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 1-nt gapped DNA in state 1 conformer 3 with disordered DNA at the shoulder
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 1-nt gapped DNA in state 2 conformer 2 with less bent DNA
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped DNA in state 2 conformer 1 with fully open clamp and unsettled DNA
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped DNA in state 2 conformer 3 with partially closed clamp
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped DNA in state 2 conformer 2 with fully open clamp and settled DNA
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped DNA in state 1 the DNA recognition state
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped DNA in state 2 conformer 5 with fully closed clamp
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped DNA in state 2 conformer 6 with fully closed clamp
Cryo-EM map of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped DNA in state 2 conformer 4 with fully closed clamp
High-resolution cryo-EM structure of human Polo-like kinase 1 in complex with onvansertib
Cryo-EM structure of AsCas12a in complex with crDNA and RNA target
3D reconstruction of Themis:Grb2:ProMacrobody256 after 3D classification (Class 3)
3D reconstruction of Themis:ProMacrobody256 after 3D classification (Class 2)
CryoEM structure of the Themis:Grb2 complex with bound ProMacrobody 256
3D reconstruction of Themis:Grb2:ProMacrobody256 after 3D classification (Class 4)
3D reconstruction of Themis:ProMacrobody256 after 3D classification (Class 1)
3D reconstruction of Themis:Grb2:ProMacrobody256 after 3D classification (Class 1)
CryoEM structure of the Themis:Grb2 complex with bound ProMacrobody 256, local refinement
3D reconstruction of Themis:Grb2:ProMacrobody256 after 3D classification (Class 2)
Cryo-EM structure of alphaM/beta2 headpiece complex without alphaM I-domain - the consensus map from alphaM/beta2:C3d-anti-CR3-Nb headpiece complex
Cryo-electron tomography of an A549 cell infected with influenza A/WSN/33 virus
Cryo-electron tomography of an A549 cell infected with influenza A/WSN/33 virus
De novo initial transcribing RNA polymerase on T7A1 promoter (weak downstream)
De novo initial transcribing RNA polymerase with 2-mer RNA and bound CTP / Michaelis complex (RPitc2+CTP)
De novo initial transcribing RNA polymerase with 5-mer RNA AUCUA (RPitc5b)
De novo initial transcribing RNA polymerase with pretranslocated 3-mer RNA / product complex (RPitc3)
De novo initial transcribing RNA polymerase with 9-mer RNA (RPitc9)
De novo initial transcribing RNA polymerase with sigma 70 region 1.1 bound (RPitc-s70_1.1)
De novo initial transcribing RNA polymerase on T7A1 promoter (empty channel)
de novo initial transcribing RNA polymerase with 5-mer RNA CCAUC (RPitc5a)
Structure of the two-pore domain, outwardly rectifying potassium (TOK1) from Candida albicans, overall structure
Structure of the two-pore domain, outwardly rectifying potassium (TOK1) from Candida albicans, Down conformation
Structure of the two-pore domain, outwardly rectifying potassium (TOK1) from Candida albicans, Up conformation
Cryo-EM structure of the TNF-alpha-Ozoralizumab (OZR)-HSA complex
TNF-alpha in complex with the TNF-alpha inhibitor Ozoralizumab (OZR)
Cryo-EM structure of SARS CoV2 S protein with stabilising mutations
Cryo-EM structure of Dengue virus serotype2 THSTI/TRC/01 strain bound with D14.F25.SO2 fab
Structural Analysis of a Plant Glycoside Hydrolase Family 116 Glucosyl Ceramidase by Cryogenic Electron Microscopy (Cryo-EM)
Helical Reconstruction of DENV2 US/BID-V594/2006 tubular particles bound with D14.F25.S02 fab
split variant of Aquifex aeolicus lumazine synthase-derived nucleocapsid variant NC-4
Cryo-EM Structure of Nipah Virus Polymerase in complex with ERDRP-0519
Cryo-EM Structure of Measles Virus Polymerase in complex with ERDRP-0519
Cryo-EM Structure of Peste Des Petits Ruminants Virus Polymerase in complex with ERDRP-0519
Cryo-EM structure of Measles Virus L Protein bound by Phosphoprotein Tetramer
Cryo-EM structure of mouse heavy-chain apoferritin on continuous carbon from 300 kV Titan Krios
Cryo-EM structure of Peste Des Petits Ruminants Virus L Protein bound by Phosphoprotein Tetramer
Cryo-EM structure of mouse heavy-chain apoferritin on continuous carbon from 200 kV Glacios
SARS-CoV-2 Omicron BA.1 spike protein in complex with a self-assembling trivalent nanobody Tr67
The TMD structure of native mouse AMPAR with 2 TARPs 2 CNIHs and PRRT1/SynDIG4
The LBD-TMD structure of native mouse AMPAR with 2 TARPs 2 CNIHs and PRRT1/SynDIG4
The LBD-TMD structure of native mouse AMPAR with 3 TARPs 1 CNIH and PRRT1/SynDIG4
Ca2+-bound MthK WT in lipid nanodiscs composed of 14:1PC (75%) and POPG (25%)
Ca2+-bound MthK WT in lipid nanodiscs composed of 22:1PC (75%) and POPG (25%)
CryoEM structure of the 41-kDa Thermus thermophilus HSP70 nucleotide-binding domain at 3.79 Angstrom resolution reveals the bound AMP-PNP and large-scale domain rearrangement
Negative stain map of A/California/07/2009 H1N1 HA in complex with 33_C08 IgG
Negative stain map of A/California/07/2009 H1N1 HA in complex with 88_B4 IgG
Negative stain map of A/California/07/2009 H1N1 HA in complex with 18_D11 IgG
ArsB from L. ferriphilum in presence of arsenite (reconstruction II)
Negative stain map of A/New York/631/1996 H3N2 HA in complex with 97_F7 IgG
Negative stain map of A/New York/631/1996 H3N2 HA in complex with 33_C08 IgG
Negative stain map of A/New York/631/1996 H3N2 HA in complex with 18_D11 IgG
Negative stain map of A/California/07/2009 H1N1 HA in complex with 97_F7 IgG
Negative stain map of A/California/07/2009 H1N1 HA in complex with 49_C09 IgG
Negative stain map of A/California/07/2009 H1N1 HA in complex with 33_C02 IgG
Negative stain map of A/New York/631/1996 H3N2 HA in complex with 88_B4 IgG
ArsB from L. ferriphilum in presence of arsenite (reconstruction I)
Negative stain map of A/California/07/2009 H1N1 HA in complex with 3_H2 IgG
Map of the Drt3a-ncRNA subcomplex in the EcDRT3 complex with ddATP and dCTP
Giraffe KIF5A motor domain in nucleotide free state bound to microtubule
Cryo-EM structure of Shewanella putrefaciens ComEC in complex with ssDNA
Cryo-EM structure of Shewanella putrefaciens ComEC in complex with dsDNA
Epitope and functional classification of human neutralizing antibodies against SFTSV Gn
Epitope and functional classification of human neutralizing antibodies against SFTSV Gn
Epitope and functional classification of human neutralizing antibodies against SFTSV Gn
Structure of PfENT1(T144C,K375C,N60R,Q266R) with inosine- outward-facing state
TRiC purified from bovine flagellar, focused refinement on E-domain
DENV2 non-structural protein 1 (NS1) Stable Tetramer complexed with Heparin
DENV2 non-structural protein 1 (NS1) Stable Tetramer Conformation 1
DENV2 non-structural protein 1 (NS1) with C-terminal mVenus Conformation 2
80S rabbit ribosome in complex with alpha-1-antitrypsin nascent chain on the P-site tRNA
DENV2 non-structural protein 1 (NS1) Loose Tetramer Conformation 1
DENV2 non-structural protein 1 (NS1) Stable Tetramer Conformation 2
DENV2 non-structural protein 1 (NS1) with C-terminal mVenus Conformation 1
DENV2 non-structural protein 1 (NS1) Loose Tetramer Conformation 2
Stabilized complex of Chlamydia trachomatic efector CT622 in complex with human WD40 domain of ATG16L1
DENV2 non-structural protein 1 (NS1) with C-terminal mVenus fusion
Structure of substrate-engaged single-cap human proteasome in state EA1
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state ED2.1
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state ED1.2
Structure of substrate-engaged double-cap human proteasome in state EA1-EA1
Structure of substrate-engaged single-cap human proteasome in state EB
Structure of substrate-engaged single-cap human proteasome in state EC1
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state ED2.3
Structure of substrate-engaged single-cap human proteasome in state EC2
Structure of substrate-engaged single-cap human proteasome in state ED0
Consensus map of human 26S proteasome in EA1-EA1 double-cap state (EMD-62090), also serving as focused map on the 20S core particle region via pseudo-single cap extraction strategy with C2/D2 symmetry
A focused map of the human 26S proteasome in the EA1-EA1 double-cap state (EMD-62090), focusing on the 19S regulatory particle region.
Structure of substrate-engaged single-cap human proteasome in state ED1
Structure of substrate-engaged single-cap human proteasome in state ED2
A focused map of the human 26S proteasome in the EA1-EA1 double-cap state (EMD-62090), focusing on the 19S regulatory particle region.
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state ED2.2
Structure of substrate-engaged single-cap human proteasome in state EA2
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state ED1.3
Human vault protein - local refinement of the waist - primed conformation
Cryo-EM structure of the tubular mastigoneme (the central tube) from golden algae 2.17 angstrom resolution
Microtubule obtained by in situ cryo-electron tomography (cryo-ET) and subtomogram averaging of mouse brain tissue
Ribosomes on the endoplasmic reticulum membrane obtained by in situ cryo-electron tomography (cryo-ET) and subtomogram averaging of mouse brain tissue
Cytosolic ribosomes obtained by in situ cryo-electron tomography (cryo-ET) and subtomogram averaging of mouse brain tissue
Structure of substrate-engaged 26S proteasome RP-CP subcomplex in state EA1.2
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state EB.1
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state EA2.3
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state EC2
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state EB.3
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state EA1.1
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state EA1.0
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state EA2.2
Structure of substrate-engaged 26S proteasome RP-CP subcomplex in state EB.2
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state ED0.1
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state EC1
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state EA2.1
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state ED1.1
Structure of substrate-engaged human 26S proteasome RP-CP subcomplex in state ED0.3
