Jean Jakoncic

I am the lead scientist at the highly Automated Macromolecular Crystallography beamline AMX at the NSLS-II storage ring synchrotron. At AMX, we currently focus the beam to an area of 7x5 μm 2 with a measured flux of 4.2 10 12 ph.s -1 at the sample position (13.5 keV). Users routinely collect data from crystals as small as 5 microns in one direction. These beam characteristics together with the high framing rate detector available to users (Eiger 9M running at up to 238 Hz) have enabled data collection from crystals of the most challenging projects. For some projects, data must be collected from dozens to hundreds to even thousands of micro- crystals for solving the 3D crystal structure. At AMX, users, with scientific support from expert beamline scientists often collect data from difficult samples; crystallized from either very large complex or very difficult to obtain small crystals, or poorly diffracting crystals at other facilities (small and intense beam allow to locate a good diffracting volume yielding complete data other impossible at other facilities). At AMX, we have the perfect instruments and the expertise to collect data from many crystals, either at room temperature or gaseous nitrogen temperature (100 K) using commercial sample holders and in-house developed sample holders. I’m a crystallographer with extensive expertise in all fields involved in MX encompassing crystallization, data collection, structure solution, molecular structure refinement, structural interpretation, X-ray instrumentation, automation, X-ray detector, X-ray methods, sample visualization, high-energy data collection, low-energy data collection, beamline construction as well as high performance computing deployment to support highly parallel computing for near instant feedback (required for a large fraction of the data collected at our 2 MX beamlines at the NSLS-II, AMX & FMX) and for advanced data processing for multiple to serial crystals data collection across multiple visits requiring hierarchical cluster analysis to sort these many data sets into fewer but useful complete data sets enabling either structure solution otherwise impossible or accessing valuable information about protein dynamics. I have solved or significantly contributed to more than 100 structures and co-authored more than 70 articles including small molecules/protein studies and de-novostructure solution using multiple crystals data collection at low energy for experimental phasing purposes relying on anomalous scattering from low Z elements. Over the last few years (eight) I worked on the planning, design, construction, commissioning and now since 5 years on the user operation of 2 state of the art macromolecular crystallography beamlines at the National Synchrotron Light Source II. These 2 beamlines are fitted with advanced autonomous automounters that, combined with the computing and software in place allow for complete automation, from sample mounting to partial structure refinement for most of the day-to-day samples. Additionally, with colleagues and collaborators, we are tackling multiple crystals (across multiple visits) data collection and data processing using dedicated pipelines. Considering that the instrument/computing I'm working on will enable automated structure solution starting from crystals, will deal with multiple crystals data collection and my extensive experience in collecting data and solving structure from challenging projects, I believe that we will achieve, when required, 1000 screened samples per day, a necessary target to enable structure solution for the most challenging projects and for achieving dynamical states of flexible proteins.