9qum

Structure of lysozyme by continuous serial electron diffraction (SerialED)

Method: ELECTRON CRYSTALLOGRAPHY Dmax: 47.9 Å Quality: GOOD

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

Lysozyme C

OrganismNot specified

UniProt P00698

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 1–147 Not recorded ACT ACETATE ION × 1 CL CHLORIDE ION × 3 ELECTRON CRYSTALLOGRAPHY cryo-EM buffer:pH 4.5;Crystals were produced by adding 1 part of lysozyme solution (40 mg/mL) to 1 part of precipitant (0.8 M NaNO3, 50mM NaAc, pH 4.5) cryo-EM vitrification conditions:Cryogen ETHANE;Manual blotting in room temperature with ambient humidity Resolution 0.83 Å R-free 0.206

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.

1320 other PDB entries and 1450 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYSC_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–147; UniProt 1–147

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 9qum

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9qum
Deposition date deposition_date2025-04-10
最后修订 last_revision2026-04-22
Structure title titleStructure of lysozyme by continuous serial electron diffraction (SerialED)
Keywords keywordsserial electron diffraction, SerialED, lysozyme, Hydrolase; HYDROLASE
Experimental Method methodELECTRON CRYSTALLOGRAPHY

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

Radius of gyration Rg (Guinier) rg_guinier14.84
Radius of gyration Rg (electron density) rg_electron13.56
Forward intensity I(0) i04755210.00
Molecular weight molecular_weight14356.0 kDa
Excluded volume excluded_volume17383 ų
Envelope volume envelope_volume18577 ų
Hydration-shell volume shell_volume11690 ų
Envelope diameter envelope_diameter45.9
Shell Rg shell_rg19.22
Envelope Rg envelope_rg13.88
Shape Rg shape_rg13.54
Total Rg total_rg14.65
Total atoms total_atoms1943
Residues n_residues129
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 dmax47.9
Rg (real space) rg_real14.76
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real4.7550e+06
I(0) uncertainty (real space) i0_real_error5.5100e+04
Rg (reciprocal space) rg_reciprocal14.77
I(0) (reciprocal space) i0_reciprocal4755000.0000
Solution quality estimate total_estimate0.8878
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.196
Kurtosis Kurtosis kurtosis-0.309
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha756200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)