The 3D structure of the apo-pseudoazurin (copper free pseudoazurin) fr
om Alcaligenes faecalis strain S-6 is determined and refined at pH 6.7
using X-ray diffraction data to 1.85 Angstrom resolution. The final c
rystallographic R-factor is 0.164. Comparing the structures of apo-pse
udoazurin and the native (CU2+) protein, we observed limited differenc
es ranging between 0.1-0.4 Angstrom at the vicinity of the copper site
, at the loops connecting the secondary structural elements, at certai
n beta-strands and at the amino and carboxy termini of the protein.