Plug-and-play polymer microfluidic chips for hydrated, room temperature, fixed-target serial crystallography
Deepshika Gilbile, Megan L. Shelby, Artem Y. Lyubimov, Jennifer L. Wierman, Diana C. F. Monteiro, Aina E. Cohen, Silvia Russi, Matthew A. Coleman, Matthias Frank, Tonya L. Kuhl
Abstract
protein crystallization (to eliminate crystal handling) or crystal slurry loading, with prepared samples stable for weeks in a humidified environment and for several hours in ambient conditions. Serial oscillation crystallography, using a multi-crystal rotational data collection approach, at a microfocus synchrotron beamline (SSRL, beamline 12-1) was used to benchmark the performance of the chips. High-resolution structures (1.3-2.7 Å) were collected from five different proteins - hen egg white lysozyme, thaumatin, bovine liver catalase, concanavalin-A (type VI), and SARS-CoV-2 nonstructural protein NSP5. Overall, our modular fabrication approach enables precise control over the cross-section of materials in the X-ray beam path and facilitates chip adaption to different sample and beamline requirements for user-friendly, straightforward diffraction measurements at room temperature.