F. G. Kozielski

This study characterizes the oligomeric state and structure of nsp10 from SARS, MERS, and SARS-CoV-2 using biochemical and biophysical methods, revealing it is predominantly monomeric and globular.

This paper demonstrates a method to identify multiple binding orientations of small molecule fragments using anomalous signals from sulphur and chlorine atoms, applied to SARS-CoV-2 nsp1 fragments.

This study analyzes NSP10 variants in SARS-CoV-2 using genomic data and biophysical methods, finding limited functional changes and strong conservation in its interactions with NSP14 and NSP16.

The paper reports the crystal structures of a humanised A33 Fab antibody variant targeting colorectal cancer, focusing on structural features of the grafted CDRs and switch linker.

This study identifies two ligand-binding sites on SARS-CoV-2 nsp1 using X-ray crystallography and fragment-based screening, offering a foundation for inhibitor development.