Programs and Communities
The collection collates collections by schools, centers, programs, and research groups.
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- Creators: Mihaleva, Galina
- Creators: School of Molecular Sciences
Description
The ASU School of Dance presents Transition Projects, February 19-21, with works by dance faculty and undergrad students, performed at Dance Studio Theatre, PEBE 132.
ContributorsRamey, Alyssa Noel (Choreographer, Dancer, Costume designer) / Mills, Lorne (Musician) / Swayze, William (Musician) / Vining, Robin (Musician) / Ammerman, Mark C. (Lighting designer, Set designer) / Mumford, Jessica (Choreographer, Costume designer, Set designer) / West, Misty (Dancer) / Rosenkrans, Angela (Choreographer) / McGloin, Aaron (Lighting designer, Choreographer, Costume designer, Set designer) / Jones, Patricia (Costume designer) / Jones, Jessica (Dancer, Dancer) / Ramey, Jenna (Dancer, Dancer) / Fitzgerald, Mary (Choreographer, Costume designer) / Abruzzi, Lucio (Dancer, Costume designer, Choreographer, Set designer) / Koch, Carolyn (Lighting designer) / Conder, Carley (Choreographer) / Syslo, Celine (Dancer, Costume designer, Dancer) / Grabianowski, Nicole (Dancer, Costume designer) / Mihaleva, Galina (Costume designer) / Franco, Mandy (Dancer) / Gersony, Alyssa (Dancer) / Hauk, Chelsey (Dancer) / McCaskill, Katie (Dancer) / McNamara, Caitlyn (Dancer) / McHale, Samantha (Dancer)
Created2010
Description
The ASU School of Dance presents Emerging Artists I, November 20-22, with works by dance MFA candidates Sammy Stephens, Jr. and LaShonda L. Williams, performed at the Dance Lab, FAC 122.
ContributorsHerberger Institute School of Dance (Publisher) / Vissicaro, Pegge (Choreographer) / Stephens, Jr., Sammy (Dancer, Choreographer, Composer) / Williams, Lashonda (Dancer, Choreographer, Costume designer, Set designer) / Mihaleva, Galina (Costume designer) / Church, Micaela (Dancer, Musician) / Croitoru, Michael (Dancer) / Fletcher, Kasey (Dancer) / Frost, Randi (Dancer) / Hood, Brittany (Dancer) / Millizer, Emily (Dancer, Musician) / Newman, Emily (Dancer) / Richards, Brittany (Dancer) / Zakrzewski, Emily (Dancer) / Ammerman, Mark C. (Set designer) / Davis, Omilade (Musician, Dancer) / Kaplan, Robert (Composer) / Benard, Jaqueline (Costume designer) / Castro, Angel (Dancer) / Gillie, Randy (Dancer) / Gonzalez, Anthony (Dancer) / Mayes, Paige (Dancer) / Schneider, Samantha (Dancer) / Wrobel, Tara (Dancer) / Aguirre, Alex (Dancer) / Nuvayestewa, Lorin (Dancer)
Created2009
Description
The ASU School of Dance presents Transition Projects II, February 20-22, with works by dance faculty and undergrad students, performed at Dance Studio Theatre, PEBE 132.
ContributorsAbruzzi, Lucio (Dancer) / Ammerman, Mark C. (Set designer) / Clegg, Debbie (Costume designer) / Conder, Carley (Choreographer, Costume designer) / Davis, Jeff (Lighting designer) / Endicott, Jenna (Dancer) / Fisher, Rose (Choreographer, Costume designer, Dancer) / Hendrix, Robbia (Dancer) / Hood, Brittany (Dancer, Choreographer, Lighting designer, Costume designer) / Jones, Jessica (Dancer) / Kirwan, Molly (Dancer) / Klassen, Katy (Dancer) / Klem, Amy (Dancer) / Koch, Carolyn (Lighting designer) / Kosowski, Jenna (Choreographer) / Kroon, Anjuli (Dancer, Choreographer, Lighting designer, Costume designer) / Lee, Yeongwen (Choreographer, Set designer) / Lopez, Lisa (Costume designer, Dancer) / Manners, Robin (Dancer) / Mansfield, Lauren (Dancer) / McGloin, Aaron (Lighting designer, Dancer) / McHale, Samantha (Dancer) / Mihaleva, Galina (Costume designer) / Murray, Leigh (Choreographer, Costume designer) / Perez, Larisa (Dancer) / Quinal, Elizabeth (Dancer) / Rosenkrans, Angela (Choreographer, Lighting designer, Costume designer) / Sheldrick, Sarah (Dancer, Choreographer, Lighting designer, Costume designer) / Smith, Chelsea (Dancer) / Theobald, Kiri (Lighting designer, Choreographer, Costume designer) / Trujillo, David (Lighting designer) / West, Misty (Dancer) / Herberger Institute School of Dance (Publisher)
Created2009
Description
The ASU School of Dance presents The Dance Annual, March 5-7, with works by dance faculty, alumni, graduate, undergraduate, and visiting artists, performed at Galvin Playhouse Theatre and Plaza.
ContributorsHerberger Institute School of Dance (Publisher) / Fitzgerald, Mary (Choreographer) / Ammerman, Mark C. (Lighting designer, Lighting designer) / Benard, Jacqueline (Costume designer, Costume designer) / Canto, Melissa (Dancer, Dancer) / Leite, Ashleigh (Choreographer) / Koch, Carolyn (Lighting designer) / Mihaleva, Galina (Costume designer, Costume designer) / Mumford, Jessica (Set designer, Videographer, Choreographer, Costume designer) / Abruzzi, Lucio (Dancer, Choreographer, Costume designer) / Grabianowski, Nicole (Dancer) / Jones, Jessica (Dancer) / Klem, Amy (Dancer) / McHale, Samantha (Dancer) / Millizer, Emily (Dancer) / Pellegrino, Laura (Dancer) / Wilcox, Madeline (Dancer) / Wrobel, Tara (Dancer, Choreographer) / Karr, Mandi (Dancer) / Zakrzewski, Emily (Dancer) / Newman, Emily (Choreographer, Dancer, Costume designer) / Fehser, Janelle (Musician, Dancer) / Trujillo, Davey (Lighting designer) / Bradley, LaTefia (Dancer) / Castro, Miguel (Dancer) / Pool, Amanda (Dancer) / Promisson, Jessica (Dancer) / Tryon, Chelsi (Dancer) / Ferrell, Rebecca A. (Choreographer) / Frost, Randi (Dancer) / McGloin, Aaron (Lighting designer) / Gonzales, Anthony (Dancer) / Ricker, Gina (Dancer) / Ramsey, Ashlee (Choreographer, Dancer) / Waugh, Whitney (Dancer) / Conder, Carley (Choreographer) / Syslo, Celine (Costume designer, Dancer) / West, Misty (Dancer) / Stephens, Jr., Sammy (Choreographer, Composer) / Aguire, Alex (Dancer) / Gillie, Randy (Dancer) / Mayes, Paige (Dancer) / Nuvayestewa, Lorin (Dancer) / Schneider, Samantha (Dancer)
Created2010
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, 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
Description
The occurrence of nonliquid and liquid physical states of submicron atmospheric particulate matter (PM) downwind of an urban region in central Amazonia was investigated. Measurements were conducted during two intensive operating periods (IOP1 and IOP2) that took place during the wet and dry seasons of the GoAmazon2014/5 campaign. Air masses representing variable influences of background conditions, urban pollution, and regional- and continental-scale biomass burning passed over the research site. As the air masses varied, particle rebound fraction, an indicator of physical state, was measured in real time at ground level using an impactor apparatus. Micrographs collected by transmission electron microscopy confirmed that liquid particles adhered, while nonliquid particles rebounded. Relative humidity (RH) was scanned to collect rebound curves.
When the apparatus RH matched ambient RH, 95 % of the particles adhered as a campaign average. Secondary organic material, produced for the most part by the oxidation of volatile organic compounds emitted from the forest, produces liquid PM over this tropical forest. During periods of anthropogenic influence, by comparison, the rebound fraction dropped to as low as 60 % at 95 % RH. Analyses of the mass spectra of the atmospheric PM by positive-matrix factorization (PMF) and of concentrations of carbon monoxide, total particle number, and oxides of nitrogen were used to identify time periods affected by anthropogenic influences, including both urban pollution and biomass burning. The occurrence of nonliquid PM at high RH correlated with these indicators of anthropogenic influence. A linear model having as output the rebound fraction and as input the PMF factor loadings explained up to 70 % of the variance in the observed rebound fractions. Anthropogenic influences can contribute to the presence of nonliquid PM in the atmospheric particle population through the combined effects of molecular species that increase viscosity when internally mixed with background PM and increased concentrations of nonliquid anthropogenic particles in external mixtures of anthropogenic and biogenic PM.
ContributorsBateman, Adam P. (Author) / Gong, Zhaoheng (Author) / Harder, Tristan H. (Author) / de Sa, Suzane S. (Author) / Wang, Bingbing (Author) / Castillo, Paulo (Author) / China, Swarup (Author) / Liu, Yingjun (Author) / O'Brien, Rachel E. (Author) / Palm, Brett B. (Author) / Shiu, Hung-Wei (Author) / Cirino, Glauber G. (Author) / Thalman, Ryan (Author) / Adachi, Kouji (Author) / Alexander, M. Lizabeth (Author) / Artaxo, Paulo (Author) / Bertram, Allan K. (Author) / Buseck, Peter (Author) / Gilles, Mary K. (Author) / Jimenez, Jose L. (Author) / Laskin, Alexander (Author) / Manzi, Antonio O. (Author) / Sedlacek, Arthur (Author) / Souza, Rodrigo A. F. (Author) / Wang, Jian (Author) / Zaveri, Rahul (Author) / Martin, Scot T. (Author) / College of Liberal Arts and Sciences (Contributor) / School of Earth and Space Exploration (Contributor) / School of Molecular Sciences (Contributor)
Created2017-02-06
Description
Carbohydrates are one of the four main building blocks of life, and are categorized as monosaccharides (sugars), oligosaccharides and polysaccharides. Each sugar can exist in two alternative anomers (in which a hydroxy group at C-1 takes different orientations) and each pair of sugars can form different epimers (isomers around the stereocentres connecting the sugars). This leads to a vast combinatorial complexity, intractable to mass spectrometry and requiring large amounts of sample for NMR characterization. Combining measurements of collision cross section with mass spectrometry (IM–MS) helps, but many isomers are still difficult to separate. Here, we show that recognition tunnelling (RT) can classify many anomers and epimers via the current fluctuations they produce when captured in a tunnel junction functionalized with recognition molecules. Most importantly, RT is a nanoscale technique utilizing sub-picomole quantities of analyte. If integrated into a nanopore, RT would provide a unique approach to sequencing linear polysaccharides.
ContributorsIm, Jong One (Author) / Biswas, Sovan (Author) / Liu, Hao (Author) / Zhao, Yanan (Author) / Sen, Suman (Author) / Biswas, Sudipta (Author) / Ashcroft, Brian (Author) / Borges, Chad (Author) / Wang, Xu (Author) / Lindsay, Stuart (Author) / Zhang, Peiming (Author) / Biodesign Institute (Contributor) / Single Molecule Biophysics (Contributor) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor) / School of Molecular Sciences (Contributor)
Created2016-12-21
Description
Crystal structure determination of biological macromolecules using the novel technique of serial femtosecond crystallography (SFX) is severely limited by the scarcity of X-ray free-electron laser (XFEL) sources. However, recent and future upgrades render microfocus beamlines at synchrotron-radiation sources suitable for room-temperature serial crystallography data collection also. Owing to the longer exposure times that are needed at synchrotrons, serial data collection is termed serial millisecond crystallography (SMX). As a result, the number of SMX experiments is growing rapidly, with a dozen experiments reported so far. Here, the first high-viscosity injector-based SMX experiments carried out at a US synchrotron source, the Advanced Photon Source (APS), are reported. Microcrystals (5–20 µm) of a wide variety of proteins, including lysozyme, thaumatin, phycocyanin, the human A[subscript 2A] adenosine receptor (A[subscript 2A]AR), the soluble fragment of the membrane lipoprotein Flpp3 and proteinase K, were screened. Crystals suspended in lipidic cubic phase (LCP) or a high-molecular-weight poly(ethylene oxide) (PEO; molecular weight 8 000 000) were delivered to the beam using a high-viscosity injector. In-house data-reduction (hit-finding) software developed at APS as well as the SFX data-reduction and analysis software suites Cheetah and CrystFEL enabled efficient on-site SMX data monitoring, reduction and processing. Complete data sets were collected for A[subscript 2A]AR, phycocyanin, Flpp3, proteinase K and lysozyme, and the structures of A[subscript 2A]AR, phycocyanin, proteinase K and lysozyme were determined at 3.2, 3.1, 2.65 and 2.05 Å resolution, respectively. The data demonstrate the feasibility of serial millisecond crystallography from 5–20 µm crystals using a high-viscosity injector at APS. The resolution of the crystal structures obtained in this study was dictated by the current flux density and crystal size, but upcoming developments in beamline optics and the planned APS-U upgrade will increase the intensity by two orders of magnitude. These developments will enable structure determination from smaller and/or weakly diffracting microcrystals.
ContributorsMartin Garcia, Jose Manuel (Author) / Conrad, Chelsie (Author) / Nelson, Garrett (Author) / Stander, Natasha (Author) / Zatsepin, Nadia (Author) / Zook, James (Author) / Zhu, Lan (Author) / Geiger, James (Author) / Chun, Eugene (Author) / Kissick, David (Author) / Hilgart, Mark C. (Author) / Ogata, Craig (Author) / Ishchenko, Andrii (Author) / Nagaratnam, Nirupa (Author) / Roy Chowdhury, Shatabdi (Author) / Coe, Jesse (Author) / Subramanian, Ganesh (Author) / Schaffer, Alexander (Author) / James, Daniel (Author) / Ketwala, Gihan (Author) / Venugopalan, Nagarajan (Author) / Xu, Shenglan (Author) / Corcoran, Stephen (Author) / Ferguson, Dale (Author) / Weierstall, Uwe (Author) / Spence, John (Author) / Cherezov, Vadim (Author) / Fromme, Petra (Author) / Fischetti, Robert F. (Author) / Liu, Wei (Author) / College of Liberal Arts and Sciences (Contributor) / School of Molecular Sciences (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / Department of Physics (Contributor)
Created2017-05-24
Description
Single-particle diffraction from X-ray Free Electron Lasers offers the potential for molecular structure determination without the need for crystallization. In an effort to further develop the technique, we present a dataset of coherent soft X-ray diffraction images of Coliphage PR772 virus, collected at the Atomic Molecular Optics (AMO) beamline with pnCCD detectors in the LAMP instrument at the Linac Coherent Light Source. The diameter of PR772 ranges from 65–70 nm, which is considerably smaller than the previously reported ~600 nm diameter Mimivirus. This reflects continued progress in XFEL-based single-particle imaging towards the single molecular imaging regime. The data set contains significantly more single particle hits than collected in previous experiments, enabling the development of improved statistical analysis, reconstruction algorithms, and quantitative metrics to determine resolution and self-consistency.
ContributorsReddy, Hemanth K. N. (Author) / Yoon, Chun Hong (Author) / Aquila, Andrew (Author) / Awel, Salah (Author) / Ayyer, Kartik (Author) / Barty, Anton (Author) / Berntsen, Peter (Author) / Bielecki, Johan (Author) / Bobkov, Sergey (Author) / Bucher, Maximilian (Author) / Carini, Gabriella A. (Author) / Carron, Sebastian (Author) / Chapman, Henry (Author) / Daurer, Benedikt (Author) / DeMirci, Hasan (Author) / Ekeberg, Tomas (Author) / Fromme, Petra (Author) / Hajdu, Janos (Author) / Hanke, Max Felix (Author) / Hart, Philip (Author) / Hogue, Brenda (Author) / Hasseinizadeh, Ahmad (Author) / Kim, Yoonhee (Author) / Kirian, Richard (Author) / Kurta, Ruslan P. (Author) / Larsson, Daniel S. D. (Author) / Loh, N. Duane (Author) / Maia, Filipe R. N. C. (Author) / Mancuso, Adrian P. (Author) / Muhlig, Kerstin (Author) / Munke, Anna (Author) / Nam, Daewoong (Author) / Nettelblad, Carl (Author) / Ourmazd, Abbas (Author) / Rose, Max (Author) / Schwander, Peter (Author) / Seibert, Marvin (Author) / Sellberg, Jonas A. (Author) / Song, Changyong (Author) / Spence, John (Author) / Svenda, Martin (Author) / van der Schot, Gijs (Author) / Vartanyants, Ivan A. (Author) / Williams, Garth J. (Author) / Xavier, P. Lourdu (Author) / ASU Biodesign Center Immunotherapy, Vaccines and Virotherapy (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / College of Liberal Arts and Sciences (Contributor) / School of Molecular Sciences (Contributor) / School of Life Sciences (Contributor) / Department of Physics (Contributor)
Created2017-06-27
Description
Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our high-resolution NMR results for a transmembrane protein, outer envelope protein of molar mass 16 kDa (OEP16), an amino acid transporter from the outer membrane of chloroplasts. Three-dimensional, high-resolution NMR experiments on the [superscript 13]C, [superscript 15]N, [superscript 2]H-triply-labeled protein were used to assign protein backbone resonances and to obtain secondary structure information. The results yield over 95% assignment of N, H[subscript N], CO, C[subscript α], and C[subscript β] chemical shifts, which is essential for obtaining a high resolution structure from NMR data. Chemical shift analysis from the assignment data reveals experimental evidence for the first time on the location of the secondary structure elements on a per residue basis. In addition T[subscript 1Z] and T[subscript 2] relaxation experiments were performed in order to better understand the protein dynamics. Arginine titration experiments yield an insight into the amino acid residues responsible for protein transporter function. The results provide the necessary basis for high-resolution structural determination of this important plant membrane protein.
ContributorsZook, James (Author) / Molugu, Trivikram R. (Author) / Jacobsen, Neil E. (Author) / Lin, Guangxin (Author) / Soll, Jurgen (Author) / Cherry, Brian (Author) / Brown, Michael F. (Author) / Fromme, Petra (Author) / Department of Chemistry and Biochemistry (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / College of Liberal Arts and Sciences (Contributor) / School of Molecular Sciences (Contributor)
Created2013-10-29