9ylx

Cryo-EM structure of the CbCash filament bound to cA4

Method: ELECTRON MICROSCOPY Dmax: 146.6 Å Quality: GOOD

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

No usable UniProt protein identity is available for this entry.

七张关系表仍保留该条目的 assembly 与组成信息,但缺少统一蛋白身份时,不能可靠建立跨 PDB 的同蛋白Chain接。

Assembly Composition of the Current Entry

Assembly Oligomeric State 实体与Construct证据 Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Homooligomer 蛋白 8 / DNA 0 / RNA 4 / 其他Polymer 0 PDB declaration: dodecameric Entity 1:CbCash × 8 Entity 2:Cyclic tetraadenylate × 4 缺少 UniProt 身份时不显示参考序列区间 Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25mM HEPES pH 7.5, 200mM NaCl, 5mM MgCl2, 1mM TCEPcryo-EM vitrification conditions:Cryogen ETHANE;Blot Force 15 Wait Time 0s Blot Time 3.5s Resolution 2.45 Å

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 9ylx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ylx
Deposition date deposition_date2025-10-09
Structure title titleCryo-EM structure of the CbCash filament bound to cA4
Keywords keywordstRNA endonuclease, cA4 activation, CRISPR associated Schlafen, Csx15, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.37
Radius of gyration Rg (electron density) rg_electron46.57
Forward intensity I(0) i01075350000.00
Molecular weight molecular_weight270030.0 kDa
Excluded volume excluded_volume337490 ų
Envelope volume envelope_volume486240 ų
Hydration-shell volume shell_volume83095 ų
Envelope diameter envelope_diameter147.3
Shell Rg shell_rg54.80
Envelope Rg envelope_rg45.35
Shape Rg shape_rg46.57
Total Rg total_rg46.85
Total atoms total_atoms18958
Residues n_residues2365
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 dmax146.6
Rg (real space) rg_real47.11
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real1.0750e+09
I(0) uncertainty (real space) i0_real_error1.8160e+07
Rg (reciprocal space) rg_reciprocal47.37
I(0) (reciprocal space) i0_reciprocal1076000000.0000
Solution quality estimate total_estimate0.8963
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.8
Skewness Skewness skewness0.069
Kurtosis Kurtosis kurtosis-0.717
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha158300000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.805

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)