Dear CHESS Community,
It is (hopefully) no secret that I hold a very special place in my heart for CHESS, the people working here, and the community it supports. With that, I am honored and delighted to join CHESS this summer as Director of MacCHESS! First, I must thank Marian Szebenyi for continuing to work with me into the fall startup - I have large shoes to fill and appreciate the overlap support. Second, I would also like to thank all who were a part of the hiring process over the past few months, plus onboarding over the last week. Much appreciated.
It is thrilling to return to the CHESS family! The ingenuity and tenacity of the CHESS spirit (the can-do attitude) speak volumes of its brilliant people.
Sincerely, I am privileged to be in your company. As you know, the intimacy of the various fields leads to a lot of crossover and feedback in techniques - you can't find that anywhere else. It truly is you, the CHESS community, who make this such a happy homecoming. I'm looking forward to supporting the team at MacCHESS, and working together to launch into the next chapter of structural biology at CHESS!
I’m heartened to see many familiar faces at CHESS, both in person and over zoom, but I recognize that there are also many new faces since I was a postdoc at CHESS. As such, I would like to share a bit about myself.
Although my family moved around quite a bit in my youth, I consider myself a Washington State native. I spent my undergraduate years in Seattle, WA pursuing Biology and Chemistry at Seattle Pacific University, and later, Honors in Physics at University of Washington (UW). After graduating, I moved across the country to Ithaca to enter Cornell’s graduate program in Biophysics where I joined Sol Gruner's lab. Applying physics to investigate structural biology really resonated with my prior experience, and I spent the majority of my graduate career studying methods to push the capabilities of macromolecular crystallography (MX). I worked closely with the MacCHESS team, gaining valuable hands-on experience, eventually specializing in serial MX. This work was only possible with the collaboration and support of the folk at CHESS. Beamtimes were an especially stimulating time, if not a bit sleep-deprived! After defending my thesis, I continued working with MacCHESS as a postdoc to implement the modifications at (then) beamline G3 for serial MX experiments.
My next opportunity came at Stanford Synchrotron Radiation Lightsource, where I worked as a staff scientist. I was an integral part of the user support staff, often assisting with data collection and processing, while maintaining the routine balance of beamline checks and optimization. Even better, I was able to dive into a few intriguing projects, such as synergistic MX and spectroscopy, serial and room temperature methods development, and beamline commissioning. I collaborated with researchers at the X-ray Free Electron Laser (XFEL) (e.g. to investigate conformational dynamics throughout catalytic cycles), but I have to admit that working so closely with an XFEL is both exciting and exhausting. Withall, I am very grateful for the experience I gained working for a DOE facility and Stanford University.
After a few years of living in the Bay Area, I then took a dramatic step away from the synchrotron radiation field to dip my toe into the biotech industry and move back to my family in the Pacific Northwest. I worked for Lumen Bioscience, a clinical-stage biotechnology company developing topically and mucosally delivered biologic drugs. The platform rests on an organism called Arthrospira Platensis, or "Spirulina" to produce edible therapeutics to treat and prevent highly prevalent diseases. I worked as the structural biology expert in the protein sciences group, but like many startups, I wore many, many hats. I gained a bevy of new skills along the way, including how to perform virtual genetic experiments, how to collaborate with big pharma, and how to make a mean espresso.
Throughout my career, my interests revolved around innovation in structural biology - pushing the limits of what we can achieve and understand of our biology. Often, this takes the form of developing new methods or new approaches to problems. For example, the MX field continues to investigate the conformational and functional landscape of proteins via an expanding set of tools. Some of the questions asked are: how do the kinetics of proteins affect their function, and do they affect how we measure structure? Are there techniques, like using high pressure, which could beneficially identify or alter the kinetics (like binding to cancer cells)? Good news! All of these questions are imminently answerable at Cornell. In collaborating with other structural biology techniques across Cornell’s campus, such as CryoEM and NMR, I'm especially eager to more fully address these and other structural questions of our users.
On a more personal note, if you catch me outside of CHESS, I will likely be trail running or backpacking in the mountains, or kayaking on a lake. I cherish the outdoors and Upstate NY is abundant with outdoor opportunities. If you don’t catch me outside of CHESS, I also like to find quiet time reading, painting, or puzzling, occasionally finding time to cook/bake. I suppose you may find evidence of that last one occasionally at CHESS too…
I look forward to working closely with each one of you and continuing the success and innovation of the CHESS community.
Best,
Jeney Wierman