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For decades, understanding the complexity of behaviors, motivations, and values has interested researchers across various disciplines. So much so that there are numerous terms, frameworks, theories, and studies devoted to understanding these complexities and how they interact and evolve into actions. However, little research has examined how employee behaviors translate

For decades, understanding the complexity of behaviors, motivations, and values has interested researchers across various disciplines. So much so that there are numerous terms, frameworks, theories, and studies devoted to understanding these complexities and how they interact and evolve into actions. However, little research has examined how employee behaviors translate into the work environment, particularly regarding perceived organizational success. This study advances research by quantitatively assessing how a greater number of individual employees’ pro-environmental behaviors are related to the perceived success of environmentally sustainable workplace activities. We have concluded that the more pro-environmental behaviors an employee embodies, the more positively they perceive the success of their local government's sustainable purchasing policy. Additionally, other factors matter, including organizational behaviors, like training, innovation, and reduction of red tape.

ContributorsFox, Angela (Author) / Darnall, Nicole (Thesis advisor) / Bretschneider, Stuart (Committee member) / Behravesh, Shirley-Ann (Committee member) / School of Sustainability (Contributor)
Created2022-04-19
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Description

BACKGROUND: The City of Phoenix initiated the HeatReady program in 2018 to prepare for extreme heat, as there was no official tool, framework, or mechanism at the city level to manage extreme heat. The current landscape of heat safety culture in schools, which are critical community hubs, has received less

BACKGROUND: The City of Phoenix initiated the HeatReady program in 2018 to prepare for extreme heat, as there was no official tool, framework, or mechanism at the city level to manage extreme heat. The current landscape of heat safety culture in schools, which are critical community hubs, has received less illumination. HeatReady Schools—a critical component of a HeatReady City—are those that are increasingly able to identify, prepare for, mitigate, track, and respond to the negative impacts of schoolgrounds heat. However, minimal attention has been given to formalize heat preparedness in schools to mitigate high temperatures and health concerns in schoolchildren, a heat-vulnerable population. This study set out to understand heat perceptions, (re)actions, and recommendations of key stakeholders and to identify critical themes around heat readiness. METHODS: An exploratory sequential mixed-methods case study approach was used. These methods focused on acquiring new insight on heat perceptions at elementary schools through semi-structured interviews using thematic analysis and the Delphi panel. Participants included public health professionals and school community members at two elementary schools—one public charter, one public—in South Phoenix, Arizona, a region that has been burdened historically with inequitable distribution of heat resources due to environmental racism and injustices. RESULTS: Findings demonstrated that 1) current heat safety resources are available but not fully utilized within the school sites, 2) expert opinions support that extreme heat readiness plans must account for site-specific needs, particularly education as a first step, and 3) students are negatively impacted by the effects of extreme heat, whether direct or indirect, both inside and outside the classroom. CONCLUSIONS: From key informant interviews and a Delphi panel, a list of 30 final recommendations were developed as important actions to be taken to become “HeatReady.” Future work will apply these recommendations in a HeatReady School Growth Tool that schools can tailor be to their individual needs to improve heat safety and protection measures at schools.

ContributorsShortridge, Adora (Author) / Walker, William VI (Author) / White, Dave (Committee member) / Guardaro, Melissa (Committee member) / Hondula, David M. (Committee member) / Vanos, Jennifer (Committee member) / School of Sustainability (Contributor)
Created2022-04-18
Description

ASU’s waste diversion goal is 90% by the fiscal year 2025 and will require collaboration across many departments and programs to be successful. Reducing plastic use, especially single-use plastic, is critical in reaching 90% waste diversion in the supply chain. To reduce supply chain single-use plastics, ASU will need the

ASU’s waste diversion goal is 90% by the fiscal year 2025 and will require collaboration across many departments and programs to be successful. Reducing plastic use, especially single-use plastic, is critical in reaching 90% waste diversion in the supply chain. To reduce supply chain single-use plastics, ASU will need the cooperation of suppliers on efforts like piloting plastic free packaging programs, packaging take back programs, alternative packaging opportunities, or promoting alternative products that contain little-to-no single-use plastic. Creating a proposed approach through identifying strategic external partners, a high-level approach to implementation, and obstacles will impact how future goals and policies are set. Determining impact and added value of the project will help cultivate support from leadership, internal stakeholders, and suppliers. The project focus will include multiple deliverables, but the final output will be a timeline that maps out what plastic streams to eliminate and when to help ASU reach their waste diversion goals. It begins with “low-hanging fruit” like straws and plastic bags and ends with a university free from all non-essential single-use plastic.

ContributorsHarper, Trevor (Author) / Hegde, Sakshi (Author) / McCrossan, Nico (Author) / Knaggs, Cecilia (Author) / Pyne, Chloe (Author) / School of Sustainability (Contributor)
Created2022-05
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Description

ASU’s waste diversion goal is 90% by the fiscal year 2025 and will require collaboration across many departments and programs to be successful. Reducing plastic use, especially single-use plastic, is critical in reaching 90% waste diversion in the supply chain. To reduce supply chain single-use plastics, ASU will need the

ASU’s waste diversion goal is 90% by the fiscal year 2025 and will require collaboration across many departments and programs to be successful. Reducing plastic use, especially single-use plastic, is critical in reaching 90% waste diversion in the supply chain. To reduce supply chain single-use plastics, ASU will need the cooperation of suppliers on efforts like piloting plastic free packaging programs, packaging take back programs, alternative packaging opportunities, or promoting alternative products that contain little-to-no single-use plastic. Creating a proposed approach through identifying strategic external partners, a high-level approach to implementation, and obstacles will impact how future goals and policies are set. Determining impact and added value of the project will help cultivate support from leadership, internal stakeholders, and suppliers. The project focus will include multiple deliverables, but the final output will be a timeline that maps out what plastic streams to eliminate and when to help ASU reach their waste diversion goals. It begins with “low-hanging fruit” like straws and plastic bags and ends with a university free from all non-essential single-use plastic.

ContributorsHarper, Trevor (Author) / Hegde, Sakshi (Author) / Knaggs, Cecilia (Author) / McCrossan, Nico (Author) / Pyne, Chloe (Author) / School of Sustainability (Contributor)
Created2022-05
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Description

ASU’s waste diversion goal is 90% by the fiscal year 2025 and will require collaboration across many departments and programs to be successful. Reducing plastic use, especially single-use plastic, is critical in reaching 90% waste diversion in the supply chain. To reduce supply chain single-use plastics, ASU will need the

ASU’s waste diversion goal is 90% by the fiscal year 2025 and will require collaboration across many departments and programs to be successful. Reducing plastic use, especially single-use plastic, is critical in reaching 90% waste diversion in the supply chain. To reduce supply chain single-use plastics, ASU will need the cooperation of suppliers on efforts like piloting plastic free packaging programs, packaging take back programs, alternative packaging opportunities, or promoting alternative products that contain little-to-no single-use plastic. Creating a proposed approach through identifying strategic external partners, a high-level approach to implementation, and obstacles will impact how future goals and policies are set. Determining impact and added value of the project will help cultivate support from leadership, internal stakeholders, and suppliers. The project focus will include multiple deliverables, but the final output will be a timeline that maps out what plastic streams to eliminate and when to help ASU reach their waste diversion goals. It begins with “low-hanging fruit” like straws and plastic bags and ends with a university free from all non-essential single-use plastic.

ContributorsHarper, Trevor (Author) / Hegde, Sakshi (Author) / McCrossan, Nico (Author) / Knaggs, Cecilia (Author) / Pyne, Chloe (Author) / School of Sustainability (Contributor)
Created2022-05
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Description
Intense femtosecond x-ray pulses from free-electron laser sources allow the imaging of individual particles in a single shot. Early experiments at the Linac Coherent Light Source (LCLS) have led to rapid progress in the field and, so far, coherent diffractive images have been recorded from biological specimens, aerosols, and quantum

Intense femtosecond x-ray pulses from free-electron laser sources allow the imaging of individual particles in a single shot. Early experiments at the Linac Coherent Light Source (LCLS) have led to rapid progress in the field and, so far, coherent diffractive images have been recorded from biological specimens, aerosols, and quantum systems with a few-tens-of-nanometers resolution. In March 2014, LCLS held a workshop to discuss the scientific and technical challenges for reaching the ultimate goal of atomic resolution with single-shot coherent diffractive imaging. This paper summarizes the workshop findings and presents the roadmap toward reaching atomic resolution, 3D imaging at free-electron laser sources.
ContributorsAquila, A. (Author) / Barty, A. (Author) / Bostedt, C. (Author) / Boutet, S. (Author) / Carini, G. (Author) / dePonte, D. (Author) / Drell, P. (Author) / Doniach, S. (Author) / Downing, K. H. (Author) / Earnest, T. (Author) / Elmlund, H. (Author) / Elser, V. (Author) / Guhr, M. (Author) / Hajdu, J. (Author) / Hastings, J. (Author) / Hau-Riege, S. P. (Author) / Huang, Z. (Author) / Lattman, E. E. (Author) / Maia, F. R. N. C. (Author) / Marchesini, S. (Author) / Ourmazd, A. (Author) / Pellegrini, C. (Author) / Santra, R. (Author) / Schlichting, I. (Author) / Schroer, C. (Author) / Spence, John (Author) / Vartanyants, I. A. (Author) / Wakatsuki, S. (Author) / Weis, W. I. (Author) / Williams, G. J. (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor)
Created2015-04-21
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Description
The advent and application of the X-ray free-electron laser (XFEL) has uncovered the structures of proteins that could not previously be solved using traditional crystallography. While this new technology is powerful, optimization of the process is still needed to improve data quality and analysis efficiency. One area is sample heterogeneity,

The advent and application of the X-ray free-electron laser (XFEL) has uncovered the structures of proteins that could not previously be solved using traditional crystallography. While this new technology is powerful, optimization of the process is still needed to improve data quality and analysis efficiency. One area is sample heterogeneity, where variations in crystal size (among other factors) lead to the requirement of large data sets (and thus 10–100 mg of protein) for determining accurate structure factors. To decrease sample dispersity, we developed a high-throughput microfluidic sorter operating on the principle of dielectrophoresis, whereby polydisperse particles can be transported into various fluid streams for size fractionation. Using this microsorter, we isolated several milliliters of photosystem I nanocrystal fractions ranging from 200 to 600 nm in size as characterized by dynamic light scattering, nanoparticle tracking, and electron microscopy. Sorted nanocrystals were delivered in a liquid jet via the gas dynamic virtual nozzle into the path of the XFEL at the Linac Coherent Light Source. We obtained diffraction to ∼4 Å resolution, indicating that the small crystals were not damaged by the sorting process. We also observed the shape transforms of photosystem I nanocrystals, demonstrating that our device can optimize data collection for the shape transform-based phasing method. Using simulations, we show that narrow crystal size distributions can significantly improve merged data quality in serial crystallography. From this proof-of-concept work, we expect that the automated size-sorting of protein crystals will become an important step for sample production by reducing the amount of protein needed for a high quality final structure and the development of novel phasing methods that exploit inter-Bragg reflection intensities or use variations in beam intensity for radiation damage-induced phasing. This method will also permit an analysis of the dependence of crystal quality on crystal size.
ContributorsAbdallah, Bahige (Author) / Zatsepin, Nadia (Author) / Roy Chowdhury, Shatabdi (Author) / Coe, Jesse (Author) / Conrad, Chelsie (Author) / Dorner, Katerina (Author) / Sierra, Raymond G. (Author) / Stevenson, Hilary P. (Author) / Camacho Alanis, Fernanda (Author) / Grant, Thomas D. (Author) / Nelson, Garrett (Author) / James, Daniel (Author) / Calero, Guillermo (Author) / Wachter, Rebekka (Author) / Spence, John (Author) / Weierstall, Uwe (Author) / Fromme, Petra (Author) / Ros, Alexandra (Author) / Department of Chemistry and Biochemistry (Contributor) / College of Liberal Arts and Sciences (Contributor) / School of Molecular Sciences (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / Department of Physics (Contributor)
Created2015-08-19
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Description
Toward the end of his career, Zewail developed strong interest in fast electron spectroscopy and imaging, a field to which he made important contributions toward his aim of making molecular movies free of radiation damage. We therefore compare here the atomistic mechanisms leading to destruction of protein samples in diffract-and-destroy

Toward the end of his career, Zewail developed strong interest in fast electron spectroscopy and imaging, a field to which he made important contributions toward his aim of making molecular movies free of radiation damage. We therefore compare here the atomistic mechanisms leading to destruction of protein samples in diffract-and-destroy experiments for the cases of high-energy electron beam irradiation and X-ray laser pulses. The damage processes and their time-scales are compared and relevant elastic, inelastic, and photoelectron cross sections are given. Inelastic mean-free paths for ejected electrons at very low energies in insulators are compared with the bioparticle size. The dose rate and structural damage rate for electrons are found to be much lower, allowing longer pulses, reduced beam current, and Coulomb interactions for the formation of smaller probes. High-angle electron scattering from the nucleus, which has no parallel in the X-ray case, tracks the slowly moving nuclei during the explosion, just as the gain of the XFEL (X-ray free-electron laser) has no parallel in the electron case. Despite reduced damage and much larger elastic scattering cross sections in the electron case, leading to not dissimilar elastic scattering rates (when account is taken of the greatly increased incident XFEL fluence), progress for single-particle electron diffraction is seen to depend on the effort to reduce emittance growth due to Coulomb interactions, and so allow formation of intense sub-micron beams no larger than a virus.
ContributorsSpence, John (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor)
Created2017-06-01
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Description
Current hard X-ray free-electron laser (XFEL) sources can deliver doses to biological macromolecules well exceeding 1 GGy, in timescales of a few tens of femtoseconds. During the pulse, photoionization can reach the point of saturation in which certain atomic species in the sample lose most of their electrons. This electronic

Current hard X-ray free-electron laser (XFEL) sources can deliver doses to biological macromolecules well exceeding 1 GGy, in timescales of a few tens of femtoseconds. During the pulse, photoionization can reach the point of saturation in which certain atomic species in the sample lose most of their electrons. This electronic radiation damage causes the atomic scattering factors to change, affecting, in particular, the heavy atoms, due to their higher photoabsorption cross sections. Here, it is shown that experimental serial femtosecond crystallography data collected with an extremely bright XFEL source exhibit a reduction of the effective scattering power of the sulfur atoms in a native protein. Quantitative methods are developed to retrieve information on the effective ionization of the damaged atomic species from experimental data, and the implications of utilizing new phasing methods which can take advantage of this localized radiation damage are discussed.
ContributorsGalli, L. (Author) / Son, S.-K. (Author) / Klinge, M. (Author) / Bajt, S. (Author) / Barty, A. (Author) / Bean, R. (Author) / Betzel, C. (Author) / Beyerlein, K. R. (Author) / Caleman, C. (Author) / Doak, R. B. (Author) / Duszenko, M. (Author) / Fleckenstein, H. (Author) / Gati, C. (Author) / Hunt, B. (Author) / Kirian, R. A. (Author) / Liang, M. (Author) / Nanao, M. H. (Author) / Nass, K. (Author) / Oberthur, D. (Author) / Redecke, L. (Author) / Shoeman, R. (Author) / Stellato, F. (Author) / Yoon, C. H. (Author) / White, T. A. (Author) / Yefanov, O. (Author) / Spence, John (Author) / Chapman, H. N. (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor)
Created2015-04-29
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Description
CTB-MPR is a fusion protein between the B subunit of cholera toxin (CTB) and the membrane-proximal region of gp41 (MPR), the transmembrane envelope protein of Human immunodeficiency virus 1 (HIV-1), and has previously been shown to induce the production of anti-HIV-1 antibodies with antiviral functions. To further improve the design

CTB-MPR is a fusion protein between the B subunit of cholera toxin (CTB) and the membrane-proximal region of gp41 (MPR), the transmembrane envelope protein of Human immunodeficiency virus 1 (HIV-1), and has previously been shown to induce the production of anti-HIV-1 antibodies with antiviral functions. To further improve the design of this candidate vaccine, X-ray crystallography experiments were performed to obtain structural information about this fusion protein. Several variants of CTB-MPR were designed, constructed and recombinantly expressed in Escherichia coli. The first variant contained a flexible GPGP linker between CTB and MPR, and yielded crystals that diffracted to a resolution of 2.3 Å, but only the CTB region was detected in the electron-density map. A second variant, in which the CTB was directly attached to MPR, was shown to destabilize pentamer formation. A third construct containing a polyalanine linker between CTB and MPR proved to stabilize the pentameric form of the protein during purification. The purification procedure was shown to produce a homogeneously pure and monodisperse sample for crystallization. Initial crystallization experiments led to pseudo-crystals which were ordered in only two dimensions and were disordered in the third dimension. Nanocrystals obtained using the same precipitant showed promising X-ray diffraction to 5 Å resolution in femtosecond nanocrystallography experiments at the Linac Coherent Light Source at the SLAC National Accelerator Laboratory. The results demonstrate the utility of femtosecond X-ray crystallography to enable structural analysis based on nano/microcrystals of a protein for which no macroscopic crystals ordered in three dimensions have been observed before.
ContributorsLee, Ho-Hsien (Author) / Cherni, Irene (Author) / Yu, HongQi (Author) / Fromme, Raimund (Author) / Doran, Jeffrey (Author) / Grotjohann, Ingo (Author) / Mittman, Michele (Author) / Basu, Shibom (Author) / Deb, Arpan (Author) / Dorner, Katerina (Author) / Aquila, Andrew (Author) / Barty, Anton (Author) / Boutet, Sebastien (Author) / Chapman, Henry N. (Author) / Doak, R. Bruce (Author) / Hunter, Mark (Author) / James, Daniel (Author) / Kirian, Richard (Author) / Kupitz, Christopher (Author) / Lawrence, Robert (Author) / Liu, Haiguang (Author) / Nass, Karol (Author) / Schlichting, Ilme (Author) / Schmidt, Kevin (Author) / Seibert, M. Marvin (Author) / Shoeman, Robert L. (Author) / Spence, John (Author) / Stellato, Francesco (Author) / Weierstall, Uwe (Author) / Williams, Garth J. (Author) / Yoon, Chun Hong (Author) / Wang, Dingjie (Author) / Zatsepin, Nadia (Author) / Hogue, Brenda (Author) / Matoba, Nobuyuki (Author) / Fromme, Petra (Author) / Mor, Tsafrir (Author) / ASU Biodesign Center Immunotherapy, Vaccines and Virotherapy (Contributor) / Department of Chemistry and Biochemistry (Contributor) / College of Liberal Arts and Sciences (Contributor) / School of Life Sciences (Contributor) / Biodesign Institute (Contributor) / Infectious Diseases and Vaccinology (Contributor) / Department of Physics (Contributor)
Created2014-08-20