7s38

Cas9:sgRNA:DNA (S. pyogenes) forming a 3-base-pair R-loop

Method: ELECTRON MICROSCOPY Dmax: 121.8 Å Quality: GOOD

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 P; UniProt 1–1368 Mutation:T1337C Non-target DNA strand × 1 Single-guide RNA × 1 Target DNA strand × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 2
Chains and sequence ranges Author chain P; PDBConstruct 4–1371; 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 7s38

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7s38
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7s38
Deposition date deposition_date2021-09-04
Structure title titleCas9:sgRNA:DNA (S. pyogenes) forming a 3-base-pair R-loop
Keywords keywordsDNase, complex, ribonucleoprotein, genome editor, HYDROLASE-RNA-DNA complex; HYDROLASE/RNA/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.28
Radius of gyration Rg (electron density) rg_electron38.60
Forward intensity I(0) i0785609000.00
Molecular weight molecular_weight201070.0 kDa
Excluded volume excluded_volume239970 ų
Envelope volume envelope_volume355410 ų
Hydration-shell volume shell_volume73914 ų
Envelope diameter envelope_diameter124.9
Shell Rg shell_rg47.17
Envelope Rg envelope_rg37.34
Shape Rg shape_rg38.60
Total Rg total_rg39.05
Total atoms total_atoms13987
Residues n_residues1491
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 dmax121.8
Rg (real space) rg_real38.98
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real7.8560e+08
I(0) uncertainty (real space) i0_real_error1.3510e+07
Rg (reciprocal space) rg_reciprocal39.17
I(0) (reciprocal space) i0_reciprocal785800000.0000
Solution quality estimate total_estimate0.8973
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.505
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77750000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)