Spain BAG for the 3D structure determination and dynamics of biological and non-biological samples using SSX and TR-SSX methods.

DOI

This BAG proposal aims to advance SX studies at ID29. We will investigate the structural dynamics and reaction mechanisms of enzymes and materials relevant to human health and biocatalysis. Our studies focus on AnmK, which catalyzes peptidoglycan recycling in P. aeruginosa; human Fascin1, an actin-bundling protein linked to cancer metastasis; NQO1, a flavoenzyme involved in antioxidant defense; and FNR/FPR, key electron transfer proteins with distinct NADP+/H binding properties. Additionally, we will study FFTR enzymes and purine-metabolizing IMPDH/GMPR to understand their regulatory mechanisms. Beyond enzymes, we propose pump-probe TR experiments on MOFs to capture structural transitions during catalysis and activation. Crystallization and preliminary diffraction tests were performed at ID29, confirming sample quality. Using ID29’s diverse sample delivery methods, we will employ SSX and TR-SX techniques to capture reaction intermediates and conformational transitions in these systems.

Identifier
DOI https://doi.org/10.15151/ESRF-ES-2216733456
Metadata Access https://icatplus.esrf.fr/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatplus.esrf.fr:inv/2216733456
Provenance
Creator JOSE MANUEL MARTIN GARCIA ORCID logo; Isabel QUEREDA MORALEDA; Daniele DE SANCTIS ORCID logo; Celia LOZANO VALLHONRAT; Monica BALSERA ORCID logo
Publisher ESRF (European Synchrotron Radiation Facility)
Publication Year 2028
Rights CC-BY-4.0; https://creativecommons.org/licenses/by/4.0
OpenAccess true
Representation
Resource Type Data from large facility measurement; Collection
Discipline Particles, Nuclei and Fields