Dr. Cremades completed her post-doctoral studies in the lab of Professor Christopher M. Dobson at the University of Cambridge in the UK working on disease-related protein misfolding and amyloid aggregation (clumping). She is the first person to isolate and purify a stable population of alpha-synuclein oligomers (assemblies of a protein). Her expertise in biophysical techniques, such as analytical ultracentrifugation (technique used to analyze biosamples), atomic force microscopy (produces very high resolution images), fourier transform infrared spectroscopy (measures absorption of different chemicals) and cryoelectron microscopy (collects high resolution images under very cold temperatures), allowed her to show that these oligomers are composed of an average of 29 alpha-synuclein molecules in an antiparallel beta sheet (type of protein structure). These oligomers produce robust reactive oxygen species (molecules that can damage DNA). Dr. Cremades also developed a new single-molecule intermolecular fluorescence resonance energy transfer (measures distance between atoms) approach to study protein misfolding and aggregation (published in Cell); this work is patented. Dr. Cremades' work will help precisely define the alpha-synuclein structures responsible for seeding and toxicity.