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)Map of M. pneumoniae 50S PTC flipped out, P in chloramphenicol-treated cells
Map of M. pneumoniae 70S EF-Tu A/T,P,E in chloramphenicol-treated cells
Map of M. pneumoniae 70S trigger factor in chloramphenicol-treated cells
Map of M. pneumoniae 70S EF-Tu A/T,P in chloramphenicol-treated cells
Map of H. sapiens 60S large ribosomal subunit with Sec61-TRAP-OSTA translocon
Map of M. pneumoniae 30S iT-TC (stable) in pseudouridimycin-treated cells
Map of M. pneumoniae 70S EF-Tu A/T,P,E in fidaxomicin-treated cells
Map of M. pneumoniae 70S trigger factor in fidaxomicin-treated cells
Consensus map of M. pneumoniae 30S small ribosomal subunit in chloramphenicol-treated cells
Consensus map of M. pneumoniae 70S ribosome in chloramphenicol-treated cells
Consensus map of M. pneumoniae 50S large ribosomal subunit in chloramphenicol-treated cells
Map of M. pneumoniae 30S iT-TC (flexible) in chloramphenicol-treated cells
Map of M. pneumoniae 50S empty/factorless in chloramphenicol-treated cells
Map of M. pneumoniae 70S membrane complex in fidaxomicin-treated cells
Structure of histone H1 in an import-chaperone complex with importin beta and importin 7
Cryo-EM structure of Clostridium perfringens pili CppA in complex with CppB
Flagellar motor structure from Borrelia burgdorferi DflhG mutant by subvolume averaging
Focused map of the external DII domain of RUVBL2 in complex with DPCD
Focused map of the external DII domain of RUVBL2 in complex with DPCD
Cryo-EM structure of human CCDC103/DNAAF19 in complex with RUVBL1/2
Focused map of the external DII domain of RUVBL2 in complex with DPCD
Focused map of human DNAAF19-RUVBL1/2 without the external DII domains.
Focused map of the external DII domain of RUVBL2 in complex with DPCD
Ribosome-dome complex including the Sec-translocon (SecYEG-SecA-SecDF) from antibiotics treated Mycoplasma pneumoniae cells (Combined)
Closed conformation dome complex including the Sec-translocon (SecYEG-SecA-SecDF) in untreated Mycoplasma pneumoniae cells
Focused map of the external DII domain of RUVBL2 in complex with DPCD
Open conformation dome complex including the Sec-translocon (SecYEG-SecA-SecDF) in untreated Mycoplasma pneumoniae cells
Cryo-EM structure of UBA6 in complex with FAT10 in the pre-adenylation state.
Cryo-EM structure of UBA6-UbDha-UBE2Z trapped ternary complex (singly loaded)
Cryo-EM structure of UBA6-UbDha-UBE2Z trapped ternary complex (doubly loaded)
Cryo-EM structure of UBA6 in complex with FAT10 in the post-thiolation state.
CryoEM structure of monoclonal Fab 047-09 1A02 binding the lateral patch of influenza virus H1 HA (A/California/04/2009 H1N1)
Murine RNF213 bound to maltoheptaose (Focused refinement of ATPase domain)
Murine RNF213 bound to maltoheptaose (Focused refinement of E3 module)
Murine RNF213 bound to maltoheptaose (Focused refinement of CBM20 domain)
Murine RNF213 bound to maltoheptaose (Focused refinement of top of stalk)
Murine RNF213 bound to maltoheptaose (Focused refinement of stalk)
Murine RNF213 bound to maltoheptaose (Focused refinement of E3 shell)
Cryo-EM structure of 3-methylcrotonyl-CoA carboxylase (MCC) complex (CT-engaged BCCP state) from Mycobacterium smegmatis
Cryo-EM structure of 3-methylcrotonyl- CoA carboxylase (MCC) complex (BC-engage BCCP state) from Mycobacterium smegmatis
Mouse 80S ribosome, eL41 KO (sg2 C11), weak P/E-site tRNA, weak P/E-site tRNA
Cryo-EM structure of 3-methylcrotonyl-CoA carboxylase (MCC) complex (BC-engaged BCCP state)from Mycobacterium smegmatis
Structure of alpha subunit of class Ib Ribonucleotide reductase in Mycobacteria (apo form)
cryo-EM structure of PSII D1-S264V from Thermosynechococcus vestitus BP-1
cryo-EM structure of PSII PsbA3-S264V in complex with DCMU from Thermosynechococcus vestitus BP-1
Cryo-EM Structure of the 12-Mer ATPase Complex YsaN from the Type III Secretion System of Yersinia enterocolitica
Cryo-EM structure of PSII PsbA3-S264V from Thermosynechococcus vestitus BP-1 (local refinement)
Cryo-EM structure of PI3Kalpha E542K mutation in complex with STX-478
Cryo-EM structure of PI3Kalpha H1047R mutation in complex with STX-478
Cryo-EM structure of PI3Kalpha E545K mutation in complex with STX-478
Cryo-EM structure of the Arabidopsis thaliana C4S4M4-type PSII supercomplex
Cryo-EM structure of the Arabidopsis thaliana C2S2M2-type PSII supercomplex
Fusion protein of Helicoverpa armigera nucleopolyhedrovirus in the uncleaved prefusion state
Structure of the intial complex in filament assembly at 3.31 angstroms resolution, conformation 1.
Structure of dimeric Tribolium castaneum (Tc) PINK1 L552R mutant in prime-activation conformation
Structure of dimeric phosphomimetic mutant of Tribolium castaneum (Tc) PINK1
Structure of dimeric autoinhibited Tribolium castaneum (Tc) PINK1 L552R mutant in complex with Ca2+
Structure of dimeric Tribolium castaneum (Tc) PINK1 L552R mutant in complex with Ca2+
Structure of dimeric autoinhibited Tribolium castaneum (Tc) PINK1 L552R mutant
LPT translocon complex from Flavobacter johnsoniae - focus volume, membrane and extracellular regions
LPT translocon complex from Flavobacter johnsoniae - consensus volume
LPT translocon complex from Flavobacter johnsoniae - focus volume, periplasmic regions
CD4 binding site and gp41-base mouse polyclonal antibodies in complex with BG505 GT1.1 SOSIP following saRNA construct GR2 immunization
CD4 binding site mouse polyclonal antibodies in complex with BG505 GT1.1 SOSIP following saRNA construct GR14 immunization
Structure of Human Argonaute2-miR200b RISC bound to 13nt long target in closed conformation
Structure of Human Argonaute2-miR200b RISC bound to 30nt long target RNA
Structure of Human Argonaute2-miR200b RISC bound to 13nt long target in open conformation
CD4 binding site mouse polyclonal antibodies in complex with BG505 GT1.1 SOSIP following saRNA construct GR6 immunization
CD4 binding site mouse polyclonal antibodies in complex with BG505 GT1.1 SOSIP following saRNA construct GR16 immunization
Structure of Human Argonaute2-miR200b RISC bound to 14nt long target in complex with kinase CK1alpha
Structure of Human Argonaute2-miR200b RISC bound to 14nt long target RNA
Structure of Human Argonaute2-miR200b RISC bound to 30nt long target in complex with kinase CK1alpha
Cryo-EM structure of Nitrogenase MoFe protein from Methanosarcina acetivorans bound to the NifI inhibitor complex in strictly anaerobic condition
Local Refinement of agonist/PAM bound mGluR8 chain B CRD and TMD when in complex with beta-arrestin-1
Local refinement of agonist-bound mGluR8 CRD and TMD in complex to G protein heterotrimer
Local Refinement of mGluR8 LBD when in complex with beta-arrestin-1
Local refinement of LBD of mGluR8 bound to agonist, PAM, and G proteins
Local refinement of agonist/PAM bound mGluR8 chain A LBD and CRD when in complex with beta-arrestin-1
Consensus non-uniform refinement map of agonist/PAM bound mGluR8 in complex with beta-arrestin-1
Local Refinement of mGluR8 TMD and G protein heterotrimer in complex
Local Refinement of G protein heterotrimer bound to scFv14 when in complex with active mGluR8
Cryo-EM structure of NifI free Nitrogenase MoFe protein from Methanosarcina acetivorans
Non-uniform refinement consensus map of mGluR8 bound to agonist, PAM, and G protein heterotrimer
Cryo EM structure of a formate acetyltransferase (PFL) from Amygdalobacter nucleatus in complex with CoA
GluA2-STZ desensitized state with partial agonist FW at 25 degrees C (full-length composite)
GluA2-STZ pre-active state with partial agonist kainic acid (KA) at 25 degrees C (full-length composite)
GluA2-STZ desensitized state with partial agonist NOW at 25 degrees C (full-length composite)
GluA2-STZ pre-active state with partial agonist NOW at 25 degrees C (full-length composite)
GluA2-STZ open state with partial agonist NOW at 25 degrees C (full-length composite)
GluA2-STZ desensitized state with partial agonist FW at 25 degrees C (ATD only)
GluA2-STZ open state with partial agonist IW at 25 degrees C (full-length composite)
GluA2-STZ open state with full agonist glutamate (Glu) at 25 degrees C (full-length composite)
GluA2-STZ open state with partial agonist FW at 25 degrees C (full-length composite)
GluA2-STZ desensitized state with full agonist glutamate (Glu) at 25 degrees C (full-length composite)
GluA2-STZ desensitized state with partial agonist FW at 25 degrees C (LBD-TMD only)
GluA2-STZ desensitized state with partial agonist FW at 25 degrees C (consensus)
GluA2-STZ open state with partial agonist FW at 25 degrees C (ATD only)
GluA2-STZ pre-active state with partial agonist kainic acid (KA) at 25 degrees C (consensus)
GluA2-STZ open state with partial agonist FW at 25 degrees C (consensus)
GluA2-STZ open state with partial agonist IW at 25 degrees C (LBD-TMD only)
GluA2-STZ pre-active state with partial agonist kainic acid (KA) at 25 degrees C (LBD-TMD only)
GluA2-STZ desensitized state with partial agonist NOW at 25 degrees C (TMD only)
GluA2-STZ desensitized state with partial agonist NOW at 25 degrees C (ATD only)
GluA2-STZ open state with partial agonist FW at 25 degrees C (LBD-TMD only)
GluA2-STZ open state with partial agonist NOW at 25 degrees C (consensus)
GluA2-STZ open state with partial agonist IW at 25 degrees C (consensus)
GluA2-STZ pre-active state with partial agonist kainic acid (KA) at 25 degrees C (ATD only)
GluA2-STZ open state with partial agonist IW at 25 degrees C (ATD only)
GluA2-STZ pre-active state with partial agonist NOW at 25 degrees C (LBD-TMD only)
GluA2-STZ open state with partial agonist NOW at 25 degrees C (LBD-TMD only)
GluA2-STZ pre-active state with partial agonist NOW at 25 degrees C (ATD only)
GluA2-STZ desensitized state with partial agonist NOW at 25 degrees C (consensus)
GluA2-STZ open state with partial agonist NOW at 25 degrees C (ATD only)
GluA2-STZ pre-active state with partial agonist NOW at 25 degrees C (consensus)
GluA2-STZ desensitized state with full agonist glutamate (Glu) at 25 degrees C (ATD only)
GluA2-STZ desensitized state with full agonist glutamate (Glu) at 25 degrees C (consensus)
GluA2-STZ desensitized state with full agonist glutamate (Glu) at 25 degrees C (LBD-TMD only)
GluA2-STZ open state with full agonist glutamate (Glu) at 25 degrees C (consensus)
GluA2-STZ open state with full agonist glutamate (Glu) at 25 degrees C (TMD only)
GluA2-STZ open state with full agonist glutamate (Glu) at 25 degrees C (LBD-TMD only)
Cryo-EM structure of Nitrogenase MoFe protein from Methanosarcina acetivorans bound to the NifI inhibitor complex in C3 symmetry
GluA2-STZ open state with full agonist glutamate (Glu) at 25 degrees C (ATD only)
GluA2-STZ desensitized state with full agonist glutamate (Glu) at 25 degrees C (TMD only)
The spike protein of HCoV-OC43 obtained from data collected on 100 kV Tundra at 180kX magnification with Falcon C detector
RNA polymerase II on Super pause sequence in the pre-translocated state
The spike protein of HCoV-OC43 obtained from data collected on 100 kV Tundra at 230 kX magnification with Falcon C detector
RNA polymerase II on Super pause sequence in the sidetracked state
Cryo-EM structure of trimeric Nitrogenase MoFe protein from Methanosarcina acetivorans
Structure of the CX3CL1.44-US28-GqiN18-scFv16 in the E-state, chemokine domain fully modeled
Structure of the CX3CL1.44-US28-GqiN18-scFv16 in the C'-state with AHD visible
Structure of the CX3CL1.44-US28-GqiN18-scFv16 in the C-state, full chemokine domain modeled
E.coli ribosome reconstruction from frames 1-40, not dose weighted
human type ribosome reconstruction from frames 1-20, not dose weighted
E.coli ribosome reconstruction from frames 1-20, not dose weighted
human type ribosome reconstruction from frames 1-40, not dose weighted
E.coli ribosome reconstruction from frames 1-80, not dose weighted
gp39 protein from Escherichia phage vB_EcoS_NBD2, unbent tubule, helix refine consensus map
gp39 protein from Escherichia phage vB_EcoS_NBD2, unbent tubule, focused map 2
gp39 protein from Escherichia phage vB_EcoS_NBD2, unbent tubule, focused map 1
sx20S complex (NSF-alphaSNAP-syntaxin-1a), non-hydrolyzing, class 1
sx20S complex (NSF-alphaSNAP-syntaxin-1a), 4:4 alphaSNAP-syntaxin-1a subcomplex local refinement, non-hydrolyzing, class 1
Cryo-EM structure of trimeric Nitrogenase MoFe protein from Methanosarcina acetivorans bound to the NifI inhibitor complex
Neurotensin Receptor 1 (NTSR1) bound to Octotensin in complex with Gi3 in the Canonical Orientation
Neurotensin Receptor 1 (NTSR1) bound to Octotensin in complex with Gi3 in the Non-Canonical Orientation
Structure of HCoV-229E spike proteins on virions by subtomogram averaging: RBD-closed and S2-compact
CryoEM structure of carbon monoxide dehydrogenase from Ruminococcus flavefaciens
Structure of HCoV-229E spike proteins on virions by subtomogram averaging: RBD-closed and S2-loose
Human Slo1-Charybdotoxin complex under divalent chelated condition - gating ring masked map
Human Slo1-PenitremA complex under divalent chelated condition - gating-ring masked out
Human Slo1-PenitremA complex under divalent chelated condition - full model
Human Slo1-Charybdotoxin complex under divalent chelated condition
Human Slo1-Iberiotoxin complex under divalent chelated condition - gating ring masked map
Human Slo1-Paxilline complex under divalent chelated condition - gating-ring masked
Human Slo1-paxilline complex under divalent chelated condition - full model
Consensus map of M. pneumoniae 50S large ribosomal subunit in native cells
Consensus map of M. pneumoniae 30S small ribosomal subunit in native cells
Map of M. pneumoniae 70S transertion-like (flexible RNAP) in native cells
Map of M. pneumoniae 30S iT-TC (flexible) in pseudouridimycin-treated cells
Map of M. pneumoniae 50S membrane complex in pseudouridimycin-treated cells
Map of M. pneumoniae 70S A/P,P/E, EF-G in pseudouridimycin-treated cells
Map of M. pneumoniae 50S membrane complex in fidaxomicin-treated cells
Map of M. pneumoniae 30S empty/factorless in fidaxomicin-treated cells
Map of M. pneumoniae 50S empty/factorless in fidaxomicin-treated cells
Map of M. pneumoniae 70S membrane complex in chloramphenicol-treated cells
Map of M. pneumoniae 30S iT-TC (flexible RNAP recentered subset) in pseudouridimycin-treated cells
Map of M. pneumoniae 70S transertion-like (collided RNAP) in pseudouridimycin-treated cells
Map of M. pneumoniae 30S iT-TC (flexible) in fidaxomicin-treated cells
Map of M. pneumoniae 50S membrane complex in chloramphenicol-treated cells
Map of M. pneumoniae 30S iT-TC (flexible RNAP recentered subset) in native cells
Map of M. pneumoniae 70S transertion-like (stable RNAP) in native cells
Map of M. pneumoniae 70S transertion-like (collided RNAP) in native cells
Consensus map of M. pneumoniae 30S small ribosomal subunit in pseudouridimycin-treated cells
Map of M. pneumoniae 70S eT-TC (flexible RNAP recentered subset) in native cells
Consensus map of M. pneumoniae 70S ribosome in pseudouridimycin-treated cells
Map of M. pneumoniae 50S RRF, EF-G in pseudouridimycin-treated cells
Map of M. pneumoniae 30S IF1/3 tRNA in pseudouridimycin-treated cells
Map of M. pneumoniae 50S empty/factorless in pseudouridimycin-treated cells
Consensus map of M. pneumoniae 50S large ribosomal subunit in pseudouridimycin-treated cells
Map of M. pneumoniae 30S empty/factorless in pseudouridimycin-treated cells
Map of M. pneumoniae 30S IF1/2/3 tRNA in pseudouridimycin-treated cells
Map of M. pneumoniae 50S trigger factor in pseudouridimycin-treated cells
Map of M. pneumoniae 70S A/P,P/E in pseudouridimycin-treated cells
Map of M. pneumoniae 70S A*,P/E in pseudouridimycin-treated cells
Map of M. pneumoniae 50S late/inactive in pseudouridimycin-treated cells
Map of M. pneumoniae 30S IF1/2/3 in pseudouridimycin-treated cells
Map of M. pneumoniae 70S dome complex in pseudouridimycin-treated cells
Map of M. pneumoniae 70S A*,P/E, EF-G in pseudouridimycin-treated cells
Map of M. pneumoniae 70S EF-Tu A/T,P in pseudouridimycin-treated cells
Map of M. pneumoniae 70S EF-Tu A/T,P,E in pseudouridimycin-treated cells
Consensus map of M. pneumoniae 30S small ribosomal subunit in fidaxomicin-treated cells
Map of M. pneumoniae 70S trigger factor in pseudouridimycin-treated cells
Consensus map of M. pneumoniae 50S large ribosomal subunit in fidaxomicin-treated cells
Consensus map of M. pneumoniae 70S ribosome in fidaxomicin-treated cells
Map of M. pneumoniae 70S eT-TC (collided) in pseudouridimycin-treated cells
Map of M. pneumoniae 70S membrane complex (no RNAP) in pseudouridimycin-treated cells
Map of M. pneumoniae 30S late biogenesis in fidaxomicin-treated cells
Map of M. pneumoniae 30S iT-TC (stable) in fidaxomicin-treated cells
Map of M. pneumoniae 50S PTC flipped out in fidaxomicin-treated cells
Map of M. pneumoniae 50S trigger factor in fidaxomicin-treated cells
Map of M. pneumoniae 70S tmRNA-SmpB,P,E in fidaxomicin-treated cells
Map of M. pneumoniae 30S IF1/3 tRNA in chloramphenicol-treated cells
Map of M. pneumoniae 50S late/inactive in chloramphenicol-treated cells
Map of M. pneumoniae 30S IF2 (all, shifted) in chloramphenicol-treated cells
Map of M. pneumoniae 50S trigger factor in chloramphenicol-treated cells
Map of M. pneumoniae 30S IF2 tRNA in chloramphenicol-treated cells
Map of M. pneumoniae 30S IF1/2/3 tRNA in chloramphenicol-treated cells
Map of M. pneumoniae 70S dome complex in chloramphenicol-treated cells
Map of M. pneumoniae 70S A,P,EOUT in chloramphenicol-treated cells
Map of M. pneumoniae 50S EF-Tu A/T, tmRNA-SmpB, E in chloramphenicol-treated cells
