5o9e

Crystal structure of the Imp4-Mpp10 complex from Chaetomium thermophilum

Method: X-RAY DIFFRACTION Dmax: 87.2 Å Quality: REASONABLE

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

Putative U3 small nucleolar ribonucleoprotein

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

UniProt G0SE90

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 75–274 Not recorded Putative U3 small nucleolar ribonucleoprotein protein × 1 (G0S9I7) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;20-30 % Ethylene glycol Resolution 1.88 Å R-free 0.219

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0SE90_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–201; UniProt 75–274

Putative U3 small nucleolar ribonucleoprotein protein

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

UniProt G0S9I7

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 433–562 Not recorded Putative U3 small nucleolar ribonucleoprotein × 1 (G0SE90) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;20-30 % Ethylene glycol Resolution 1.88 Å R-free 0.219

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S9I7_CHATD
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–131; UniProt 433–562

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 5o9e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5o9e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5o9e
Deposition date deposition_date2017-06-19
Structure title titleCrystal structure of the Imp4-Mpp10 complex from Chaetomium thermophilum
Keywords keywordsRibosome biogenesis, RIBOSOME, BRIX; RIBOSOME
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.58
Radius of gyration Rg (electron density) rg_electron20.54
Forward intensity I(0) i018024500.00
Molecular weight molecular_weight31961.0 kDa
Excluded volume excluded_volume40098 ų
Envelope volume envelope_volume48719 ų
Hydration-shell volume shell_volume20630 ų
Envelope diameter envelope_diameter89.4
Shell Rg shell_rg26.16
Envelope Rg envelope_rg21.32
Shape Rg shape_rg20.52
Total Rg total_rg21.39
Total atoms total_atoms2248
Residues n_residues281
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 dmax87.2
Rg (real space) rg_real21.70
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.8020e+07
I(0) uncertainty (real space) i0_real_error2.5960e+05
Rg (reciprocal space) rg_reciprocal21.67
I(0) (reciprocal space) i0_reciprocal18020000.0000
Solution quality estimate total_estimate0.5838
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.9
Skewness Skewness skewness0.689
Kurtosis Kurtosis kurtosis0.918
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3633000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.336; Stabil: 1.000; Sysdev: 0.281; Positv: 1.000; Valcen: 0.733; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)