Faculty and Staff

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.

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.

Membrane proteins are key players in biological systems, mediating signalling events and the specific transport of e.g. ions and metabolites. Consequently, membrane proteins are targeted by a large number of currently approved drugs. Understanding their functions and molecular mechanisms is greatly dependent on structural information, not least on complexes with functionally or medically important ligands. Structure determination, however, is hampered by the difficulty of obtaining well diffracting, macroscopic crystals. Here, the feasibility of X-ray free-electron-laser-based serial femtosecond crystallography (SFX) for the structure determination of membrane protein-ligand complexes using microcrystals of various native-source and recombinant P-type ATPase complexes is demonstrated. The data reveal the binding sites of a variety of ligands, including lipids and inhibitors such as the hallmark P-type ATPase inhibitor orthovanadate. By analyzing the resolution dependence of ligand densities and overall model qualities, SFX data quality metrics as well as suitable refinement procedures are discussed. Even at relatively low resolution and multiplicity, the identification of ligands can be demonstrated. This makes SFX a useful tool for ligand screening and thus for unravelling the molecular mechanisms of biologically active proteins.

Background: Interaction in the form of cooperation, communication, and friendly competition theoretically precede the development of group cohesion, which often precedes adherence to health promotion programs. The purpose of this manuscript was to explore longitudinal relationships among dimensions of group cohesion and group-interaction variables to inform and improve group-based strategies within programs aimed at promoting physical activity.

Methods: Ethnic minority women completed a group dynamics-based physical activity promotion intervention (N = 103; 73% African American; 27% Hispanic/Latina; mage = 47.89 + 8.17 years; mBMI = 34.43+ 8.07 kg/m[superscript 2]) and assessments of group cohesion and group-interaction variables at baseline, 6 months (post-program), and 12 months (follow-up).

Results: All four dimensions of group cohesion had significant (ps < 0.01) relationships with the group-interaction variables. Competition was a consistently strong predictor of cohesion, while cooperation did not demonstrate consistent patterns of prediction.

Conclusions: Facilitating a sense of friendly competition may increase engagement in physical activity programs by bolstering group cohesion.