Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects

Conclusions derived from this comparison are valid for the whole S1/P1 nuclease family. For proper model building and refinement, multiple lattice-translocation defects present in the measured diffraction data needed to be solved. Two different approaches were tested and compared. Correction of the measured intensities proved to be superior to the use of the dislocation model of asymmetric units with partial occupancy of individual chains. As the crystals suffered from multiple lattice translocations, equations for their correction were derived de novo. The presented approach to the correction of multiple lattice-translocation defects may help to solve similar problems in the field of protein X-ray crystallography.

Source: Acta Crystallographica Section D - September 27, 2022 Category: Biochemistry Authors: Ad á mkov á , K. Koval', T. Ø stergaard, L.H. Du š kov á , J. Mal ý , M. Š vecov á , L. Sk á lov á , T. Kolenko, P. Dohn á lek, J. Tags: S1 nuclease Aspergillus oryzae lattice-translocation defects nucleotides nucleosides complexes research papers Source Type: research