9zix

Cryo-EM structure of Geobacillus stearothermophilus RNase P holoenzyme in 1 mM Mg2+, conformer 20

Method: ELECTRON MICROSCOPY Dmax: 160.5 Å Quality: GOOD

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

Ribonuclease P protein component

Geobacillus stearothermophilus

UniProt A0A150N245

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 Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain B; UniProt 1–115 Not recorded RNase P RNA (417-MER) × 1 MG MAGNESIUM ION × 24 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.68 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.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A150N245_GEOSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–116; UniProt 1–115

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 9zix

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9zix
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9zix
Deposition date deposition_date2025-12-04
Structure title titleCryo-EM structure of Geobacillus stearothermophilus RNase P holoenzyme in 1 mM Mg2+, conformer 20
Keywords keywordsribozyme, RNA, RNase P., RNA-Hydrolase complex; RNA/HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.17
Radius of gyration Rg (electron density) rg_electron46.50
Forward intensity I(0) i0934254000.00
Molecular weight molecular_weight149800.0 kDa
Excluded volume excluded_volume143960 ų
Envelope volume envelope_volume255100 ų
Hydration-shell volume shell_volume49616 ų
Envelope diameter envelope_diameter167.6
Shell Rg shell_rg46.24
Envelope Rg envelope_rg45.55
Shape Rg shape_rg46.47
Total Rg total_rg46.53
Total atoms total_atoms9933
Residues n_residues533
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 dmax160.5
Rg (real space) rg_real46.54
Rg uncertainty (real space) rg_real_error2.38
I(0) (real space) i0_real9.3430e+08
I(0) uncertainty (real space) i0_real_error1.8170e+07
Rg (reciprocal space) rg_reciprocal46.17
I(0) (reciprocal space) i0_reciprocal933800000.0000
Solution quality estimate total_estimate0.8493
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.5
Skewness Skewness skewness0.480
Kurtosis Kurtosis kurtosis-0.308
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28620000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.820; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.636

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)