Biography:
I am a Senior Research Officer with more than 20 years experience of carrying out research activities across Neuroscience programmes, having joined the Medical Research Council at the Toxicology Unit in May 2003. I helped to set the first Committee for Public Engagement back in 2010 and throughout these years I have kept an active participation in the delivery of outreach activities: I thoroughly enjoy welcoming young students for working experience placements at our facility or participating in schools' careers fairs! Since 2017 I maintain professional registration with the Science Council at the Scientist level (RSc) and hold membership with the Institute of Biomedical Sciences.
Before joining the Unit I was awarded a Double Major in Biochemistry and Microbiology by the University of the Basque Country in Spain, and a Master of Biochemistry (Neurochemistry) by the Venezuelan Institute for Scientific Research, where I moved to live and work (literally, the residential hall was in the same grounds) in 1995 thanks to a grant from the Spanish Agency for International Development Cooperation.
Currently I am a qualified CREST award assessor for the British Science Association and love reading the wide variety of creative research projects that young pupils produce, which leave me always amazed; to grant them the award after so much hard work and dedication is the cherry on the cake that makes me feel like the fairy godmother in a fairy tale, and I love it! are we not all a child at heart after all?
As a good native of the Basque Country, outside of working hours you will find me in my kitchen cooking at home, or enjoying the beautiful landscapes that surround Cambridgeshire, or volunteering my time on different educational projects close to heart that help my mind to stay active and ground myself.
Research Interests:
Electron Microscopy, Ultramicrotomy, Array tomography, SBFSEM, Cryo-electron tomography, 3D cell reconstruction
While conventional electron microscopy (TEM, SEM, negative staining, Immunogold) is providing us with valuable structural and morphological information on animal and plant cells, virus and microorganisms that can be used for pathological diagnosis and localization of specific proteins, new technologies and software developments are changing the way we process samples for EM, acquire images through more sophisticated microscopes equipped with best CCD and single electron detector camera, and process images for data extraction.
Two of these new technologies are the Serial Block Face Scanning Electron Microscopy (SBFSEM) and Array Tomography, which provide additional information by their ability to section very thin slices parallel to the epoxy-resin block face where our sample has been embedded and by covering volumes of hundreds of micrometres cubic. This additional information allows us to perform three-dimensional cell volume reconstruction and carry on more extensive quantitative morphological analysis in tissue to better description of pathological diseases and effects of treatments. We are getting new insights on the spatial-functional relationships between organelles and contributing to better understanding of organelle disfunction related diseases. Disfunction in processes such as synthesis and transport of proteins through the ERGI system and lysosomal compartments, or mitochondrial related diseases that lead to cellular death, can therefore be studied at ultrastructural level making use of these novel techniques.
Another new technology that is bringing breakthroughs in the field of EM is the Cryo-electron tomography, which relays in the vitrification of biological samples for better ultrastructural preservation, the efficiency of single electron detector cameras to record events at the low-accelerating voltage that is required for these samples, and the strong computational power required to integrate the thousands of tomograms obtained by the tilting of the sample through the x-axis. Although the volume covered by this technique is lower than the one covered by SBFSEM and Array Tomography, the resolution is reached at the molecular level. Cryo-EM becomes then a wonderful technique for the study of the biomolecular complex sitting at the membranes at the active conformation, bringing mechanistic insights that can be useful applied for drug-designed pharmaceutical studies.
