› 1bwh

X-ray diffraction
1.8Å resolution

THE 1.8 A STRUCTURE OF GROUND CONTROL GROWN TETRAGONAL HEN EGG WHITE LYSOZYME

Released:
DOI: 10.2210/pdb1bwh/pdb
PDB entry 1bwh coloured by chain, front view.
PDB entry 1bwh coloured by chain, side view.
PDB entry 1bwh coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 A resolution.
Dong J, Boggon TJ, Chayen NE, Raftery J, Bi RC, Helliwell JR
Acta Crystallogr D Biol Crystallogr 55 745-52 (1999)
PMID: 10089304

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 domain:

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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 79.266Å b: 79.266Å c: 37.956Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.233

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Citations

1 review citation

Lessons from crystals grown in the Advanced Protein Crystallisation Facility for conventional crystallisation applied to structural biology.
Vergara et al. (2005)
9 other articles

6 mentions without citation

Fretting about FRET: correlation between kappa and R.
VanBeek et al. (2007)
5 more