X-ray diffraction
1.61Å resolution

SAD structure of Hen Egg White Lysozyme recovered by continuous rotation data collection and multivariate analysis of Friedel pairs

Source organism: Gallus gallus
Primary publication:
Bayesian machine learning improves single-wavelength anomalous diffraction phasing.
Acta Crystallogr A Found Adv 75 851-860 (2019)
PMID: 31692460

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 147 amino acids
Theoretical weight: 16.26 KDa
Source organism: Gallus gallus
  • Canonical: P00698 (Residues: 1-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: P43212
Unit cell:
a: 79.07Å b: 79.07Å c: 36.98Å
α: 90° β: 90° γ: 90°
R R work R free
0.142 0.141 0.167