Focus Honoring Dr. Kristina “Kicki” Håkansson, Recipient of the 2016 Biemann Medal

I the American Society for Mass Spectrometry to celebrate the t is a pleasure to introduce a special focus of the Journal of accomplishments of the 2016 Biemann Medalist Focus Honoring Dr. Kristina BKicki^ Håkansson, Recipient of the 2016 Biemann Medal Q: Many of us were inspired to pursue science by our high school teachers. What were your chemistry teachers like at school? - Kicki’s answer. My high school math, physics, and chemistry teachers were all wonderful. I was in a Bnatural sciences^ program with a high-achieving group of students. I do recall that the chemistry teacher had to give most of us the highest possible grade (5 on a scale from 1 to 5) after we took the national standardized test. One memory is that he taught us the optimal way of doing dishes. I also fondly remember the hands-on demonstrations. Q: What made you choose science for your tertiary education? Kicki’s answer. I was mainly applying to medical schools but then I received a flyer in the mail saying something like Bare you the kind of student who likes BOTH Chemistry/Biology AND Math/Physics, then this new program is for you.^ This wording resonated with me, and I applied to the new program in molecular biotechnology at the School of Engineering at Uppsala University. I was admitted to this program but not to medical school and decided to give it a try. It turns out I really liked the breadth of the courses I was taking and the overall environment in the engineering school so I stayed in the 4.5year program to earn my M.Sc. degree after doing research involving atomic force microscopy (AFM) of DNA. Q: What was your first research experiment in chemistry? Kicki’s answer. The last semester of the M.Sc. program required full-time research and a thesis. I did not know exactly what I wanted to do but attended a seminar by Bo Sundqvist (Professor of Ion Physics and cofounder of the molecular biotechnology M.Sc. program) in which he showed one of the first AFM images of an antibody. I was blown away by the fact that you could see the Y-shape of a single molecule with this technique! Following this seminar, I contacted Prof. Sundqvist, and he agreed to accept me into his laboratory (which also did a lot of mass spectrometry, but that came later). My first experiments involved figuring out the optimum buffer conditions for imaging DNA with AFM (i.e., how to avoid spaghettilike supercoiled structures that couldn’t be analyzed very well and instead get plasmids to lay down on mica as nice circular structures). Q: You moved from Sweden to the USA to pursue your postdoctoral studies and then stayed on to establish your independent research career. Tell us something about what motivated you to make such a move and why you decided to stay in the USA. Kicki’s answer. I transitioned to mass-spectrometry-based research for my Ph.D. thesis (in the same group as my M.Sc. research but under supervision of Prof. Per Hakansson; no relation). We were fortunate to receive an FT-ICR instrument about half way through my Ph.D. degree, and I was amazed by the high performance compared with the time-of-flight instruments I had worked with until then. I wanted to learn more about FT-ICR MS and was thrilled to receive an opportunity to work with one of its coinventors, Prof. Alan Marshall, for my postdoctoral research. Alan was a wonderful mentor and pushed me onto the path of an independent career. I had not considered applying for academic positions in the USA as I did not do any schooling here but he convinced me to try and was highly supportive and helpful throughout the entire process up until the moment when I had to decide between three offers. At that time, he told me he was not going to influence me one way or another. I chose to go to Michigan, and I think it only hurt him a little being a big fan of Ohio State football (I barely knew about football rivalries at the time). Q: What is your favorite piece of work that you have been involved in? Kicki’s answer. This is difficult to answer so I will list two: One is a four-way collaboration with medicinal chemists, X-ray crystallographers, and cryo-EM scientists to reveal how the structure of a 2 × 160-kDa polyketide synthase undergoes dramatic changes during its catalytic cycle depending on which small molecules are covalently loaded onto it. I loved being part of this interdisciplinary team and gaining insights into a molecular machine that previously had been viewed as a Bblack box.^ High-resolution LC/MS data were essential to figure out the covalent state of each proteoform we looked at. A favorite in my own lab was the discovery of negative-ion ECD—we were so excited when we saw the first charge-increased species! Q: Reading your papers, one get’s the impression that you like doing technically challenging experiments. Is that correct? Kicki’s answer. Absolutely—it is so rewarding when you can get all the components to work at the same time! niECD is one example—it took a long time but was real (...truncated)