7z4e

SpCas9 bound to 8-nucleotide complementary DNA substrate

Method: ELECTRON MICROSCOPY Dmax: 124.7 Å Quality: EXCELLENT

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 B; UniProt 1–1368 Mutation:D10A, H840A sgRNA × 1 Target strand of 8 nucleotide complementary DNA substrate × 1 Non-target strand of 8 nucleotide complementary DNA substrate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.14 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 B; 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 7z4e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7z4e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7z4e
Deposition date deposition_date2022-03-03
Structure title titleSpCas9 bound to 8-nucleotide complementary DNA substrate
Keywords keywordsCRISPR, Cas9, R-loop, substrate binding, off-target, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.36
Radius of gyration Rg (electron density) rg_electron39.96
Forward intensity I(0) i0789678000.00
Molecular weight molecular_weight202180.0 kDa
Excluded volume excluded_volume241180 ų
Envelope volume envelope_volume354680 ų
Hydration-shell volume shell_volume71280 ų
Envelope diameter envelope_diameter133.4
Shell Rg shell_rg48.38
Envelope Rg envelope_rg38.75
Shape Rg shape_rg39.96
Total Rg total_rg40.35
Total atoms total_atoms14069
Residues n_residues1499
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 dmax124.7
Rg (real space) rg_real40.17
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real7.8970e+08
I(0) uncertainty (real space) i0_real_error1.2800e+07
Rg (reciprocal space) rg_reciprocal40.35
I(0) (reciprocal space) i0_reciprocal789800000.0000
Solution quality estimate total_estimate0.9040
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.1
Skewness Skewness skewness0.100
Kurtosis Kurtosis kurtosis-0.547
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha75640000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)