Using advanced labeling methods developed by our group, enable us to push the NOE detection threshold an order of magnitude back compare to standard NMR approaches.
This structurally meaningful long range intermethyl NOES were crucial to determine the structure of a rare functional state of human Hsp90 ATP binding domain. By integrating NMR data and low or medium-resolution EM data, we also able to determine the self assembly pathway and the high-resolution structure of the large 468 kDa dodecameric aminopeptidase TET2.
Key Publications
“Visualizing the Transiently Populated Closed-State of Human HSP90 ATP Binding Domain" Nature Communications
“Unraveling Self-Assembly Pathways of the 468 kDa Proteolytic Machine TET2" Science Advances
“Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex" Nature Communications
