6o56

HNH Nuclease from S. pyogenes Cas9

Method: X-RAY DIFFRACTION Dmax: 74.0 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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 775–908 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;0.1 M [imidazole and MES] pH 6.5, 25% (v/v) [2-methyl-2,4-pentanediol, PEG1000, and PEG3350], 0.3 M [diethylene glycol, triethylene glycol, tetraethylene glycol, pentaethlyene glycol] Resolution 1.90 Å R-free 0.253
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 775–908 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;0.1 M [imidazole and MES] pH 6.5, 25% (v/v) [2-methyl-2,4-pentanediol, PEG1000, and PEG3350], 0.3 M [diethylene glycol, triethylene glycol, tetraethylene glycol, pentaethlyene glycol] Resolution 1.90 Å R-free 0.253

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 145 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 2–135; UniProt 775–908 Author chain B; PDBConstruct 2–135; UniProt 775–908

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 6o56

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6o56
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6o56
Deposition date deposition_date2019-03-01
Structure title titleHNH Nuclease from S. pyogenes Cas9
Keywords keywordsnuclease, CRISPR Cas9, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.28
Radius of gyration Rg (electron density) rg_electron20.60
Forward intensity I(0) i018748800.00
Molecular weight molecular_weight31920.0 kDa
Excluded volume excluded_volume39650 ų
Envelope volume envelope_volume47117 ų
Hydration-shell volume shell_volume19641 ų
Envelope diameter envelope_diameter78.6
Shell Rg shell_rg26.64
Envelope Rg envelope_rg20.92
Shape Rg shape_rg20.56
Total Rg total_rg21.51
Total atoms total_atoms2244
Residues n_residues270
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 dmax74.0
Rg (real space) rg_real21.33
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.8750e+07
I(0) uncertainty (real space) i0_real_error2.4630e+05
Rg (reciprocal space) rg_reciprocal21.32
I(0) (reciprocal space) i0_reciprocal18750000.0000
Solution quality estimate total_estimate0.7778
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.452
Kurtosis Kurtosis kurtosis-0.149
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5548000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.729; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.927; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)