Automation, Robotics and Remote Access at the SSRL Synchrotron

A Collaborative UAH Department of Biological Science and SSRL Structural Molecular Biology Workshop

9:00 am to 4:00 pm on Thursday, March 8, 2018 - Shelby Science and Technology Center, University of Alabama Huntsville

This workshop will introduce participants to the Remote Access Crystallography Program and the Small Angle Scattering Program at the SSRL synchrotron. The workshop will include lectures and hands-on crystallography training using the SSRL facilities remotely. Participants will also learn about fixed target and injector methods for serial crystallography at SSRL and the LCLS X-ray free electron laser.

Workshop organizers: Crissy Tarver (UAH), Marc Pusey (UAH), Clyde Smith (SSRL) and Aina Cohen (SSRL).

Attendance is limited.
To register please 1) send an email to Register and 2) create an account in the SSRL User Portal. After emailing your registeration request, we will respond with more information.
Participants interested in sending crystals to SSRL for data collection training on March 8th or 9th should inquire within their registration email.

Participants are encouraged to bring their own laptop computer for the hands-on session.

Tentative Schedule

Thursday, March 8th, Shelby Science and Technology Center room 301

Morning Session

9:00 Aina Cohen 'Remote access crystallography experiments at cryogenic temperatures and at controlled humidity.'

9:40 Clyde Smith 'Live remote access demonstration at SSRL'

10:30 Coffee Break (15 minutes)

10:45 Thomas Weiss 'Small Angle X-ray Scattering at SSRL'

11:30 Aina Cohen 'New opportunities for serial crystallography at SSRL and the LCLS X-ray Free Electron Laser (XFEL)'

12:10 Lunch

Afternoon Session

1:30 Concurrent hands-on sessions (15 minute coffee break at 2:40 then groups will swap between sessions)

(i) Installation of NX client software and connecting to the SSRL crystallography beamlines (Clyde Smith) Participants are encouraged to bring their own laptops.
(ii) Sample and pin preparation, and the use of SSRL cassettes, Unipucks and the new SAM microplates (Aina Cohen)

4:00 Workshop Conclusion

Getting Around UAH

Parking is available directly in front of the Shelby Science and Technology Center and in the parking garage located on Holmes Avenue. Lunch for participants will be provided by the UAH Department of Biological Science.

More information about this workshop

The Stanford Synchrotron Radiation Lightsource (SSRL) provides state-of-the-art facilities for structural biology research to the academic research community. All SSRL crystallography beam lines are fully remote accessible and offer advanced robotics for automated crystal quality screening. An intense micro-focus beamline, BL12-2, enables rapid shutterless data collection using very small crystals. A UV-Vis absorption microspectrometer is available at BL9-2 to confirm the electronic state for metalloprotein complexes and poised intermediates and to monitor specific effects of radiation exposure. BL4-2 is dedicated to small angle scattering and diffraction studies on primarily non-crystalline systems.

Up to 288 cryo-cooled crystals can be mounted by the beamline robot (the Stanford Automated Mounter, or SAM) and screened for diffraction quality in a matter of hours without human intervention. The best quality crystals can then be remounted for the collection of complete X-ray diffraction data sets. Furthermore, the entire screening and data collection experiment can be controlled from the experimenter's home laboratory by means of advanced software tools that enable network-based control of the highly automated beamlines. This remote capability is now available on all SSRL macromolecular crystallography beamlines. During the last user run, over 97% of the user groups used the SAM robot and the remote access tools, some from as far away as Australia and New Zealand. The new technologies implemented at SSRL have eliminated the distinction between remote and local access to synchrotron resources. Furthermore, new technologies will enable remote access data collection using crystals at ambient temperatures and at controlled humidity. A similar facility for serial crystallography data collection is available at the LCLS-MFX instrument.

The BL42 small-angle x-ray scattering (SAXS) station is a permanent experimental station dedicated to structural biology and biophysics, providing state-of-the-art experimental facilities for structural studies on nucleic acids, proteins, protein assemblies, virus particles, biological fibers, lipid membranes and their complexes. A recently installed Pilatus3 X 1M detector provides excellent data quality for static as well as for fast time resolved experiments (up to a time resolution of 2ms). The station features a fully automated high-throughput solution scattering setup with an attached software pipeline that automatically performs all the necessary steps for data reduction and initial analysis. For aggregation prone samples or unstable complexes a highly automated size-exclusion chromatography (SEC) setup can be directly connected to the instrument allowing in-line SEC-SAXS experiments.

During this workshop, Aina Cohen will introduce the SMB Macromolecular Crystallography Resource at SSRL and LCLS, Thomas Weiss will describe the SSRL SAXS beamline and experiments, and Clyde Smith will present a live remote access demonstration and connect to some SSRL beamlines to present the features accessible to remote users. There will also be hands-on component covering sample and pin preparation, the use of SSRL cassettes and Unipucks, installation of the NX client software, assistance with SSRL User Portal registration and obtaining User accounts.