9zq6

Structure of SpyCas9 in complex with the anti-CRISPR protein AcrIIA26

Method: ELECTRON MICROSCOPY Dmax: 122.0 Å Quality: GOOD

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

CRISPR-associated endonuclease Cas9/Csn1

Streptococcus pyogenes M1 GAS

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 Protein–RNA Heteromer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 1–1368 Not recorded AcrIIA26 × 1 sgRNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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 9zq6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9zq6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9zq6
Deposition date deposition_date2025-12-17
Structure title titleStructure of SpyCas9 in complex with the anti-CRISPR protein AcrIIA26
Keywords keywordsCRISPR, Cas9, Acr, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.33
Radius of gyration Rg (electron density) rg_electron38.40
Forward intensity I(0) i0691172000.00
Molecular weight molecular_weight198510.0 kDa
Excluded volume excluded_volume241800 ų
Envelope volume envelope_volume351190 ų
Hydration-shell volume shell_volume73859 ų
Envelope diameter envelope_diameter126.1
Shell Rg shell_rg46.70
Envelope Rg envelope_rg36.98
Shape Rg shape_rg38.37
Total Rg total_rg38.95
Total atoms total_atoms13893
Residues n_residues1559
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 dmax122.0
Rg (real space) rg_real39.01
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real6.9120e+08
I(0) uncertainty (real space) i0_real_error1.1940e+07
Rg (reciprocal space) rg_reciprocal39.21
I(0) (reciprocal space) i0_reciprocal691300000.0000
Solution quality estimate total_estimate0.8984
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.8
Skewness Skewness skewness0.078
Kurtosis Kurtosis kurtosis-0.530
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha83250000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (3)

9. Files and Curves (10)