3cka

X-ray diffraction
1.65Å resolution

The crystal structure of OspA mutant

Released:
Source organism: Borreliella burgdorferi
Primary publication:
Minimalist design of water-soluble cross-beta architecture.
Proc Natl Acad Sci U S A 107 3469-74 (2010)
PMID: 20133689

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-112108 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer Surface Protein A Chains: A, B
Molecule details ›
Chains: A, B
Length: 320 amino acids
Theoretical weight: 34.69 KDa
Source organism: Borreliella burgdorferi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D0VWU8 (Residues: 5-320; Coverage: 99%)
Sequence domains: Borrelia lipoprotein

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 75.293Å b: 83.647Å c: 106.153Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.24
Expression system: Escherichia coli BL21(DE3)