8c9a

Cryo-EM captures early ribosome assembly in action

Method: ELECTRON MICROSCOPY Dmax: 155.8 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

50S ribosomal protein L34

OrganismNot specified

UniProt P0A7P5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain 2; UniProt 1–46 Not recorded 23S rRNA × 1 50S ribosomal protein L4 × 1 (P60723) 50S ribosomal protein L22 × 1 (P61175) 50S ribosomal protein L24 × 1 (P60624) 50S ribosomal protein L29 × 1 (P0A7M6) 50S ribosomal protein L23 × 1 (P0ADZ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

464 other PDB entries and 509 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL34_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain 2; PDBConstruct 1–46; UniProt 1–46

50S ribosomal protein L4

OrganismNot specified

UniProt P60723

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain E; UniProt 1–201 Not recorded 23S rRNA × 1 50S ribosomal protein L34 × 1 (P0A7P5) 50S ribosomal protein L22 × 1 (P61175) 50S ribosomal protein L24 × 1 (P60624) 50S ribosomal protein L29 × 1 (P0A7M6) 50S ribosomal protein L23 × 1 (P0ADZ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

521 other PDB entries and 566 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL4_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–201; UniProt 1–201

50S ribosomal protein L22

OrganismNot specified

UniProt P61175

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain S; UniProt 1–110 Not recorded 23S rRNA × 1 50S ribosomal protein L34 × 1 (P0A7P5) 50S ribosomal protein L4 × 1 (P60723) 50S ribosomal protein L24 × 1 (P60624) 50S ribosomal protein L29 × 1 (P0A7M6) 50S ribosomal protein L23 × 1 (P0ADZ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

571 other PDB entries and 616 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL22_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain S; PDBConstruct 1–110; UniProt 1–110

50S ribosomal protein L24

OrganismNot specified

UniProt P60624

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain U; UniProt 1–104 Not recorded 23S rRNA × 1 50S ribosomal protein L34 × 1 (P0A7P5) 50S ribosomal protein L4 × 1 (P60723) 50S ribosomal protein L22 × 1 (P61175) 50S ribosomal protein L29 × 1 (P0A7M6) 50S ribosomal protein L23 × 1 (P0ADZ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

452 other PDB entries and 496 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL24_ECOLI
Isoform
PDB entities 5
Chains and sequence ranges Author chain U; PDBConstruct 1–104; UniProt 1–104

50S ribosomal protein L29

OrganismNot specified

UniProt P0A7M6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain Y; UniProt 1–63 Not recorded 23S rRNA × 1 50S ribosomal protein L34 × 1 (P0A7P5) 50S ribosomal protein L4 × 1 (P60723) 50S ribosomal protein L22 × 1 (P61175) 50S ribosomal protein L24 × 1 (P60624) 50S ribosomal protein L23 × 1 (P0ADZ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

457 other PDB entries and 502 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL29_ECOLI
Isoform
PDB entities 6
Chains and sequence ranges Author chain Y; PDBConstruct 1–63; UniProt 1–63

50S ribosomal protein L23

OrganismNot specified

UniProt P0ADZ0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain T; UniProt 1–100 Not recorded 23S rRNA × 1 50S ribosomal protein L34 × 1 (P0A7P5) 50S ribosomal protein L4 × 1 (P60723) 50S ribosomal protein L22 × 1 (P61175) 50S ribosomal protein L24 × 1 (P60624) 50S ribosomal protein L29 × 1 (P0A7M6) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.86 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

439 other PDB entries and 481 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL23_ECOLI
Isoform
PDB entities 7
Chains and sequence ranges Author chain T; PDBConstruct 1–100; UniProt 1–100

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8c9a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8c9a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8c9a
Deposition date deposition_date2023-01-21
Structure title titleCryo-EM captures early ribosome assembly in action
Keywords keywordsribosome, ribosome assembly, ribosome biogenesis, total reconstitution, RNA, ribosomal protein.; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier47.94
Radius of gyration Rg (electron density) rg_electron47.97
Forward intensity I(0) i02669770000.00
Molecular weight molecular_weight269830.0 kDa
Excluded volume excluded_volume270600 ų
Envelope volume envelope_volume494300 ų
Hydration-shell volume shell_volume86505 ų
Envelope diameter envelope_diameter166.9
Shell Rg shell_rg52.32
Envelope Rg envelope_rg46.28
Shape Rg shape_rg47.95
Total Rg total_rg48.10
Total atoms total_atoms18059
Residues n_residues1175
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax155.8
Rg (real space) rg_real47.75
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real2.6700e+09
I(0) uncertainty (real space) i0_real_error5.4820e+07
Rg (reciprocal space) rg_reciprocal47.93
I(0) (reciprocal space) i0_reciprocal2670000000.0000
Solution quality estimate total_estimate0.8854
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary56.7
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.406
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha116300000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.861

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)