[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleVisualizing the translation landscape in human cells at high resolution.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 10757, Year 2025
Publish dateNov 28, 2025
AuthorsWei Zheng / Yuekang Zhang / Jimin Wang / Shuhui Wang / Pengxin Chai / Elizabeth J Bailey / Chenghao Zhu / Wangbiao Guo / Swapnil C Devarkar / Shenping Wu / Jianfeng Lin / Kai Zhang / Jun Liu / Ivan B Lomakin / Yong Xiong /
PubMed AbstractComprehensive in situ structures of macromolecules can transform our understanding of biology and advance human health. Here, we map protein synthesis inside human cells in detail by combining ...Comprehensive in situ structures of macromolecules can transform our understanding of biology and advance human health. Here, we map protein synthesis inside human cells in detail by combining automated cryo-focused ion beam (FIB) milling and in situ single-particle cryo electron microscopy (cryo-EM). With this in situ cryo-EM approach, we resolved a 2.2 Å consensus structure of the human 80S ribosome and unveiled 23 functional states, nearly all better than 3 Å resolution. Compared to in vitro studies, we observed variations in ribosome structures, distinct environments of ion and polyamine binding, and associated proteins such as EDF1 and NACβ that are typically not enriched with purified ribosomes. We also detected additional peptide-related density features on the ribosome and visualized ribosome-ribosome interactions in helical polysomes. Finally, high-resolution structures from cells treated with homoharringtonine and cycloheximide revealed a distinct translational landscape and a spermidine that interacts with cycloheximide at the E site, one of the numerous polyamines that also bind native ribosomes. These results underscore the value of high-resolution in situ studies in the native environment.
External linksNat Commun / PubMed:41315256 / PubMed Central
MethodsEM (single particle)
Resolution2.19 - 3.91 Å
Structure data

EMDB-71329, PDB-9p6z:
In situ human P-Z state 80S ribosome
Method: EM (single particle) / Resolution: 2.97 Å

EMDB-71331, PDB-9p72:
In situ human P-E state 80S ribosome
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-71332, PDB-9p73:
In situ human eEF2-A/P-P/E state 80S ribosome
Method: EM (single particle) / Resolution: 2.66 Å

EMDB-71333, PDB-9p76:
In situ human eEF1A-A/T-P state 80S ribosome
Method: EM (single particle) / Resolution: 2.83 Å

EMDB-71340, PDB-9p7f:
In situ HHT and CHX treated A-P state 80S ribosome
Method: EM (single particle) / Resolution: 3.56 Å

EMDB-71341, PDB-9p7g:
In situ HHT and CHX treated A-P-Z state 80S ribosome
Method: EM (single particle) / Resolution: 3.54 Å

EMDB-71342, PDB-9p7h:
In situ HHT and CHX treated human eEF1A-A/T-P state 80S ribosome
Method: EM (single particle) / Resolution: 3.68 Å

EMDB-71343, PDB-9p7i:
In situ HHT and CHX treated human eEF1A-A/T-P-Z state 80S ribosome
Method: EM (single particle) / Resolution: 3.69 Å

EMDB-71344, PDB-9p7j:
In situ HHT and CHX treated human P state 80S ribosome
Method: EM (single particle) / Resolution: 3.91 Å

EMDB-71345, PDB-9p7k:
In situ human post eEF1A-A/T-P-E state 80S ribosome
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-71346, PDB-9p7l:
In situ human Post-eEF1A-AT-P state 80S ribosome
Method: EM (single particle) / Resolution: 2.92 Å

EMDB-71348, PDB-9p7n:
In situ human Post-eEF1A-A/T-P-Z state 80S ribosome
Method: EM (single particle) / Resolution: 2.83 Å

EMDB-71349, PDB-9p7o:
In situ human AT-P-Z state ribosome
Method: EM (single particle) / Resolution: 2.65 Å

EMDB-71355, PDB-9p7w:
In situ human A-P state 80S ribosome
Method: EM (single particle) / Resolution: 2.93 Å

EMDB-71356, PDB-9p7x:
In situ human A-P-Z state 80S ribosome
Method: EM (single particle) / Resolution: 2.83 Å

EMDB-71357, PDB-9p7y:
In situ human A-P-E state 80S ribosome
Method: EM (single particle) / Resolution: 2.75 Å

EMDB-71371, PDB-9p8b:
In situ human eEF1A-A/T-P-E state 80S ribosome
Method: EM (single particle) / Resolution: 2.48 Å

EMDB-71377, PDB-9p8h:
In situ human A/P-P/E state 80S ribosome
Method: EM (single particle) / Resolution: 2.98 Å

EMDB-71378, PDB-9p8i:
In situ HHT and CHX treated human P-Z state 80S ribosome
Method: EM (single particle) / Resolution: 3.89 Å

EMDB-71411, PDB-9p9h:
In situ human unrotated hibernating with CCDC124 state 80S ribosome
Method: EM (single particle) / Resolution: 2.84 Å

EMDB-71412, PDB-9p9i:
In situ human unrotated hibernating without CCDC124 state 80S ribosome
Method: EM (single particle) / Resolution: 2.77 Å

EMDB-71413, PDB-9p9j:
In situ human 60S ribosome
Method: EM (single particle) / Resolution: 2.87 Å

EMDB-71414, PDB-9p9k:
In situ human 60S ribosome with EIF6
Method: EM (single particle) / Resolution: 2.96 Å

EMDB-71435, PDB-9pa7:
In situ human 80S consensus ribosome with EBP1
Method: EM (single particle) / Resolution: 2.67 Å

EMDB-71440: In situ human 80S ribosome (consensus map)
Method: EM (single particle) / Resolution: 2.19 Å

EMDB-71441: In situ human 80S ribosome (focused on 60S)
Method: EM (single particle) / Resolution: 2.2 Å

EMDB-71442: In situ human 80S ribosome (Focused on 40S body)
Method: EM (single particle) / Resolution: 2.51 Å

EMDB-71443: In situ human 80S ribosome (Focused on 40S head)
Method: EM (single particle) / Resolution: 2.64 Å

EMDB-71477, PDB-9pbe:
In situ human 80S ribosome (composite map)
Method: EM (single particle) / Resolution: 2.19 Å

EMDB-71696, PDB-9pkg:
In situ human P state 80S ribosome
Method: EM (single particle) / Resolution: 3.26 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-SPM:
SPERMINE

ChemComp-SPD:
SPERMIDINE

ChemComp-ZN:
Unknown entry

ChemComp-3HE:
4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione

ChemComp-HMT:
(3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine

ChemComp-HOH:
WATER

ChemComp-K:
Unknown entry

ChemComp-PUT:
1,4-DIAMINOBUTANE

Source
  • homo sapiens (human)
KeywordsRIBOSOME / in situ / Ribsome

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more