Activity, stability and 3-D structure of the Cu( ii ) form of a chitin-active lytic polysaccharide monooxygenase from Bacillus amyloliquefaciens

, and the substrate greatly increasing the thermal stability of the enzyme. A spiral data collection strategy has been used to facilitate access to the previously unobservable Cu(ii) state of the active centre, revealing a coordination geometry around the copper which is distorted from axial symmetry, consistent with the previous findings from EPR spectroscopy.