9orz

MicroED structure of apo-form lysozyme

Method: ELECTRON CRYSTALLOGRAPHY Dmax: 51.2 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 19–147 Fragment:lyzozyme NA SODIUM ION × 1 ELECTRON CRYSTALLOGRAPHY cryo-EM buffer:pH 4.8;800 mM NaCl, 80 mM sodium acetate pH 4.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.30 Å R-free 0.250

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 1–129; UniProt 19–147

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 9orz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9orz
Deposition date deposition_date2025-05-23
Structure title titleMicroED structure of apo-form lysozyme
Keywords keywordsEnzyme, MicroED, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON CRYSTALLOGRAPHY

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

Radius of gyration Rg (Guinier) rg_guinier15.12
Radius of gyration Rg (electron density) rg_electron13.81
Forward intensity I(0) i04636800.00
Molecular weight molecular_weight14344.0 kDa
Excluded volume excluded_volume17486 ų
Envelope volume envelope_volume19072 ų
Hydration-shell volume shell_volume11829 ų
Envelope diameter envelope_diameter51.4
Shell Rg shell_rg19.49
Envelope Rg envelope_rg14.21
Shape Rg shape_rg13.78
Total Rg total_rg14.94
Total atoms total_atoms1002
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 dmax51.2
Rg (real space) rg_real15.05
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real4.6370e+06
I(0) uncertainty (real space) i0_real_error6.1460e+04
Rg (reciprocal space) rg_reciprocal15.06
I(0) (reciprocal space) i0_reciprocal4637000.0000
Solution quality estimate total_estimate0.7888
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.5
Skewness Skewness skewness0.266
Kurtosis Kurtosis kurtosis-0.153
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha815400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.753; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)