Joint X-ray/neutron structure of Lentinus similis AA9_A at room temperature.
Tobias TandrupLeila Lo LeggioFlora MeilleurPublished in: Acta crystallographica. Section F, Structural biology communications (2023)
Lytic polysaccharide monooxygenases (LPMOs) are copper metalloenzymes which cleave polysaccharides oxidatively and are important in pathogen biology, carbon cycling and biotechnology. The Lentinus similis family AA9 isoform A (LsAA9_A) has been extensively studied as a model system because its activity towards smaller soluble saccharide substrates has allowed detailed structural characterization of its interaction with a variety of substrates by X-ray crystallography at high resolution. Here, the joint X-ray/neutron room-temperature crystallographic structure of carbohydrate-free LsAA9_A in the copper(II) resting state refined against X-ray and neutron data at 2.1 and 2.8 Å resolution, respectively, is presented. The results provide an experimental determination of the protonation states of the copper(II)-coordinating residues and second-shell residues in LsAA9_A, paving the way for future neutron crystallographic studies of LPMO-carbohydrate complexes.
Keyphrases
- room temperature
- high resolution
- resting state
- dual energy
- functional connectivity
- ionic liquid
- mass spectrometry
- electron microscopy
- computed tomography
- electronic health record
- big data
- oxide nanoparticles
- magnetic resonance
- tandem mass spectrometry
- current status
- machine learning
- simultaneous determination
- cell wall