Faculty and Staff

We present results from experiments at the Linac Coherent Light Source (LCLS) demonstrating that serial femtosecond crystallography (SFX) can be performed to high resolution (~2.5 Å) using protein microcrystals deposited on an ultra-thin silicon nitride membrane and embedded in a preservation medium at room temperature. Data can be acquired at a high acquisition rate using x-ray free electron laser sources to overcome radiation damage, while sample consumption is dramatically reduced compared to flowing jet methods. We achieved a peak data acquisition rate of 10 Hz with a hit rate of ~38%, indicating that a complete data set could be acquired in about one 12-hour LCLS shift using the setup described here, or in even less time using hardware optimized for fixed target SFX. This demonstration opens the door to ultra low sample consumption SFX using the technique of diffraction-before-destruction on proteins that exist in only small quantities and/or do not produce the copious quantities of microcrystals required for flowing jet methods.

While PhD dissertations are typically accessible many other terminal degree projects remain invisible and inaccessible to a greater audience. Over the past year and a half, librarians at Arizona State University collaborated with faculty and departmental administrators across a variety of fields to develop and create institutional repository collections that highlight and authoritatively share this type of student scholarship with schools, researchers, and future employers. This poster will present the benefits, challenges, and considerations required to successfully implement and manage these collections of applied final projects or capstone projects. Specifically, issues/challenges related to metadata consistency, faculty buy-in, and developing an ingest process, as well as benefits related to increased visibility and improved educational and employment opportunities will be discussed. This interactive presentation will also discuss lessons learned from the presenter’s experiences in context of how they can easily apply to benefit their respective institutions.

Digital technology has enabled us to record and share our memories and histories faster and in greater numbers than previously imagined. However digital files rely on hardware, software, and descriptive information to be used. As formats change and equipment to read them goes out of use we are all challenged to connect our present to our future. How long do you want your digital files to last? Decades or even a few years from now will you still be able to access and enjoy those pictures, documents and other digital items you create today?

Libraries, museums and archives spend countless hours and resources preserving physical items from the past and present, but may be forfeiting the longevity of our digital work and connecting to future generations through unintended neglect. Using practical examples and employing best practices of research institutions, participants will learn important first steps to digital preservation including the importance of metadata to personal history, recommended file formats, and approaches they can immediately use to ensure the work they create today will still be enjoyed tomorrow. Help yourself, your organization, and your patrons continue to connect their digital heritage to the generations yet to come.

Previous proof-of-concept measurements on single-layer two-dimensional membrane-protein crystals performed at X-ray free-electron lasers (FELs) have demonstrated that the collection of meaningful diffraction patterns, which is not possible at synchrotrons because of radiation-damage issues, is feasible. Here, the results obtained from the analysis of a thousand single-shot, room-temperature X-ray FEL diffraction images from two-dimensional crystals of a bacteriorhodopsin mutant are reported in detail. The high redundancy in the measurements boosts the intensity signal-to-noise ratio, so that the values of the diffracted intensities can be reliably determined down to the detector-edge resolution of 4 Å. The results show that two-dimensional serial crystallography at X-ray FELs is a suitable method to study membrane proteins to near-atomic length scales at ambient temperature. The method presented here can be extended to pump–probe studies of optically triggered structural changes on submillisecond timescales in two-dimensional crystals, which allow functionally relevant large-scale motions that may be quenched in three-dimensional crystals.