Abstract
The 3D structure of the apo-pseudoazurin (copper free pseudoazurin) from Alcaligenes faecalis strain S-6 is determined and refined at pH 6.7 using X-ray diffraction data to 1.85Åresolution. The final crystallographicR-factor is 0.164. Comparing the structures of apo-pseudoazurin and the native (Cu 2+) protein, we observed limited differences ranging between 0.1–0.4Åat the vicinity of the copper site, at the loops connecting the secondary structural elements, at certain β-strands and at the amino and car☐y termini of the protein.
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