9h4m

wtCas9 bound to off-target 1 EMX1-1 (-)SC DNA minicircle

Method: ELECTRON MICROSCOPY Dmax: 122.9 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 3 RNA 1 PDB declaration: pentameric(5) Consistent with all polymer counts Chain A; UniProt 1–1368 Not recorded EMX1-1 sgRNA × 1 Target Strand Pre-Cut × 1 Non-Target Strand × 1 Target Strand Post-Cut × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 4
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 9h4m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9h4m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9h4m
Deposition date deposition_date2024-10-20
Structure title titlewtCas9 bound to off-target 1 EMX1-1 (-)SC DNA minicircle
Keywords keywordsdCas9, Cas9, off-target, EMX1-1, negatively supercoiled, diamond ring, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.43
Radius of gyration Rg (electron density) rg_electron39.06
Forward intensity I(0) i0740039000.00
Molecular weight molecular_weight195410.0 kDa
Excluded volume excluded_volume233360 ų
Envelope volume envelope_volume343130 ų
Hydration-shell volume shell_volume71178 ų
Envelope diameter envelope_diameter131.9
Shell Rg shell_rg46.82
Envelope Rg envelope_rg37.86
Shape Rg shape_rg39.06
Total Rg total_rg39.43
Total atoms total_atoms13599
Residues n_residues1454
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 dmax122.9
Rg (real space) rg_real39.19
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real7.4000e+08
I(0) uncertainty (real space) i0_real_error1.2030e+07
Rg (reciprocal space) rg_reciprocal39.34
I(0) (reciprocal space) i0_reciprocal740200000.0000
Solution quality estimate total_estimate0.8945
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.2
Skewness Skewness skewness0.176
Kurtosis Kurtosis kurtosis-0.451
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha84220000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.885

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)