9jl2

Classical conformation for the spCas9 with gRNA and target DNA complex

Method: ELECTRON MICROSCOPY Dmax: 124.1 Å Quality: REASONABLE

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

CRISPR-associated endonuclease Cas9/Csn1

Streptococcus pyogenes serotype M1

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 TS × 1 NTS × 1 gRNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 3
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 9jl2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9jl2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9jl2
Deposition date deposition_date2024-09-17
Structure title titleClassical conformation for the spCas9 with gRNA and target DNA complex
Keywords keywordsSpCas9, gRNA, Target DNA, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.83
Radius of gyration Rg (electron density) rg_electron38.67
Forward intensity I(0) i0600011000.00
Molecular weight molecular_weight172790.0 kDa
Excluded volume excluded_volume204750 ų
Envelope volume envelope_volume295700 ų
Hydration-shell volume shell_volume61959 ų
Envelope diameter envelope_diameter137.1
Shell Rg shell_rg46.16
Envelope Rg envelope_rg37.86
Shape Rg shape_rg38.68
Total Rg total_rg39.01
Total atoms total_atoms22807
Residues n_residues1259
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 dmax124.1
Rg (real space) rg_real38.66
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real6.0000e+08
I(0) uncertainty (real space) i0_real_error1.1100e+07
Rg (reciprocal space) rg_reciprocal38.77
I(0) (reciprocal space) i0_reciprocal600100000.0000
Solution quality estimate total_estimate0.6240
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary48.4
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.515
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61300000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 0.999; Sysdev: 0.132; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)