9c9p

Cas9 ternary complex, 14-nt sgRNA, State I (linear)

Method: ELECTRON MICROSCOPY Dmax: 125.0 Å Quality: GOOD

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

CRISPR-associated endonuclease Cas9/Csn1

Streptococcus pyogenes

UniProt Q99ZW2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Monomer Protein × 1 DNA 2 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–1368 Not recorded sgRNA × 1 Target strand × 1 Non-target strand × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

134 other PDB entries and 146 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAS9_STRP1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1368; UniProt 1–1368

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 9c9p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c9p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c9p
Deposition date deposition_date2024-06-14
Structure title titleCas9 ternary complex, 14-nt sgRNA, State I (linear)
Keywords keywordsType II-A CRISPR-associated endonuclease RNA-guided DNA targeting Mg2+ dependent, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.70
Radius of gyration Rg (electron density) rg_electron39.37
Forward intensity I(0) i0672489000.00
Molecular weight molecular_weight180740.0 kDa
Excluded volume excluded_volume212920 ų
Envelope volume envelope_volume334630 ų
Hydration-shell volume shell_volume69133 ų
Envelope diameter envelope_diameter132.2
Shell Rg shell_rg46.84
Envelope Rg envelope_rg38.23
Shape Rg shape_rg39.42
Total Rg total_rg39.64
Total atoms total_atoms12596
Residues n_residues1478
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 dmax125.0
Rg (real space) rg_real39.46
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real6.7250e+08
I(0) uncertainty (real space) i0_real_error1.2150e+07
Rg (reciprocal space) rg_reciprocal39.61
I(0) (reciprocal space) i0_reciprocal672600000.0000
Solution quality estimate total_estimate0.8982
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.0
Skewness Skewness skewness0.161
Kurtosis Kurtosis kurtosis-0.500
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77260000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)