Featured Customer: Kristina Djinović Carugo, Ph.D.

Kristina Djinović Carugo received her MSc in Chemistry from University of Ljubljana, Slovenia, as well as her Ph.D. in Structural Biology, performed at the University of Pavia, Italy in 1992. After a post-doctoral stage at the University of Pavia, she moved to European Molecular Biology Laboratory in Heidelberg, Germany (1995), where she stayed first as EMBO postdoctoral fellow and then as EMBL staff scientist. In 1999 she joined Elettra - Sincrotrone Trieste, Italy, where she headed the Unit of Structural Biology and Crystallography. In 2004 she moved to University of Vienna, Austria, where she holds the Chair of Molecular Structural biology and is since 2009 the Head of the Department of Structural and Computational Biology at the University of Vienna.

Please tell us about your background: where you grew up, studied, and why you chose the field you did.

My current position involves research, teaching and heading the Department, along with services to the scientific community. My main scientific interest lies in investigating the molecular mechanisms underlying the architecture and assembly of the Z-discs of the striated muscle - boundaries between adjacent sarcomeres, using integrative structural biology approach on reconstituted complexes.

Other long standing research lines revolve around structure-function analysis of metallo-enzymes involved in protection from chemical and oxidative damage and methods development for customised protein crystallisation based on biophysical properties, and for structure analysis of dynamic/disordered systems.

In what context did you first learn about light scattering and Wyatt instruments?

The first time I learnt about light scattering was during my time at EMBL-Heidelberg (1995-1999): we acquired an DLS instrument which many of us very soon started to proficiently use to assess the monodispersity of samples.

How have your Wyatt instruments contributed to your research and development studies?

We routinely use SEC-MALS to assess the molecular weight and stoichiometry of our proteins and reconstituted complexes. It has proven also very valuable in studies of intrinsically disordered proteins, where the SEC elution volumes alone can give a miss-leading information on the molecular weight. We use DLS for recurrent check of sample monodispersity and (in multi-well format) for screening for optimal buffers.