X-ray diffraction
1.3Å resolution

Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection

Source organism: Bos taurus
Primary publication:
Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection?
Acta Crystallogr. D Biol. Crystallogr. 62 125-32 (2006)
PMID: 16421442

Function and Biology Details

Reaction catalysed:
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Cationic trypsin Chain: X
Molecule details ›
Chain: X
Length: 243 amino acids
Theoretical weight: 25.44 KDa
Source organism: Bos taurus
  • Canonical: P00760 (Residues: 4-246; Coverage: 100%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 54.262Å b: 58.355Å c: 66.765Å
α: 90° β: 90° γ: 90°
R R work R free
0.106 0.105 0.139