› 2w1m

X-ray diffraction
1.78Å resolution

THE INTERDEPENDENCE OF WAVELENGTH, REDUNDANCY AND DOSE IN SULFUR SAD EXPERIMENTS: 2.070 A WAVELENGTH with 2theta 30 degrees data

Released:
DOI: 10.2210/pdb2w1m/pdb
PDB entry 2w1m coloured by chain, front view.
PDB entry 2w1m coloured by chain, side view.
PDB entry 2w1m coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
The interdependence of wavelength, redundancy and dose in sulfur SAD experiments.
Cianci M, Helliwell JR, Suzuki A
Acta Crystallogr D Biol Crystallogr 64 1196-209 (2008)
PMID: 19018096

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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132831 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P00698 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:
Ligand CL 8 x CL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P43212
Unit cell:
a: 78.243Å b: 78.243Å c: 36.978Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.18 0.238

Quick links

Citations

2 review citations

Assessing and maximizing data quality in macromolecular crystallography.
Karplus et al. (2015)
1 more

1 mention without citation

In meso in situ serial X-ray crystallography of soluble and membrane proteins.
Huang et al. (2015)