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Description

Since 2018, MMM team members have written sport-style summaries following the live "play-by-play" narration of simulated combatant encounters on social media. These summaries, highlighting key adaptations, human impacts, and other scholarly information, have been provided to educators to describe tournament outcomes to their learners who do not follow the battle

Since 2018, MMM team members have written sport-style summaries following the live "play-by-play" narration of simulated combatant encounters on social media. These summaries, highlighting key adaptations, human impacts, and other scholarly information, have been provided to educators to describe tournament outcomes to their learners who do not follow the battle narrations "live" on social media.

ContributorsLesciotto, Kate M (Author) / Martin, Jessica Leigh, 1991- (Author) / Krell, Jason (Author) / Hinde, Katie (Author, Researcher) / Anderson, Chris (Researcher) / Brokaw, Alyson F (Researcher) / Chestnut, Tara (Researcher) / Connors, Patrice K. (Researcher) / Dasari, Mauna (Researcher) / Drew, Josh (Researcher) / Durgavich, Lara (Researcher) / Hilborn, Anne W. (Researcher) / Kissel, Marc (Researcher) / Lee, Danielle N. (Researcher) / Lewton, Kristi L (Researcher) / Light, Jessica (Researcher) / Murphy, Asia (Researcher) / Tanis, Brian   (Researcher) / Varner, Jo (Researcher) / Wrenford, Kwasi (Researcher)
Created2022
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Description
Diacylglycerol kinase catalyses the ATP-dependent conversion of diacylglycerol to phosphatidic acid in the plasma membrane of Escherichia coli. The small size of this integral membrane trimer, which has 121 residues per subunit, means that available protein must be used economically to craft three catalytic and substrate-binding sites centred about the

Diacylglycerol kinase catalyses the ATP-dependent conversion of diacylglycerol to phosphatidic acid in the plasma membrane of Escherichia coli. The small size of this integral membrane trimer, which has 121 residues per subunit, means that available protein must be used economically to craft three catalytic and substrate-binding sites centred about the membrane/cytosol interface. How nature has accomplished this extraordinary feat is revealed here in a crystal structure of the kinase captured as a ternary complex with bound lipid substrate and an ATP analogue. Residues, identified as essential for activity by mutagenesis, decorate the active site and are rationalized by the ternary structure. The γ-phosphate of the ATP analogue is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane. A catalytic mechanism for this unique enzyme is proposed. The active site architecture shows clear evidence of having arisen by convergent evolution.
ContributorsLi, Dianfan (Author) / Stansfeld, Phillip J. (Author) / Sansom, Mark S. P. (Author) / Keogh, Aaron (Author) / Vogeley, Lutz (Author) / Howe, Nicole (Author) / Lyons, Joseph A. (Author) / Aragao, David (Author) / Fromme, Petra (Author) / Fromme, Raimund (Author) / Basu, Shibom (Author) / Grotjohann, Ingo (Author) / Kupitz, Christopher (Author) / Rendek, Kimberley (Author) / Weierstall, Uwe (Author) / Zatsepin, Nadia (Author) / Cherezov, Vadim (Author) / Liu, Wei (Author) / Bandaru, Sateesh (Author) / English, Niall J. (Author) / Gati, Cornelius (Author) / Barty, Anton (Author) / Yefanov, Oleksandr (Author) / Chapman, Henry N. (Author) / Diederichs, Kay (Author) / Messerschmidt, Marc (Author) / Boutet, Sebastien (Author) / Williams, Garth J. (Author) / Seibert, M. Marvin (Author) / Caffrey, Martin (Author) / College of Liberal Arts and Sciences (Contributor) / School of Molecular Sciences (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / Department of Physics (Contributor)
Created2015-12-17
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Description
Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these conformational changes. Here we report the

Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these conformational changes. Here we report the room temperature crystal structure of the chromophore-binding domains of the Deinococcus radiodurans phytochrome at 2.1 Å resolution. The structure was obtained by serial femtosecond X-ray crystallography from microcrystals at an X-ray free electron laser. We find overall good agreement compared to a crystal structure at 1.35 Å resolution derived from conventional crystallography at cryogenic temperatures, which we also report here. The thioether linkage between chromophore and protein is subject to positional ambiguity at the synchrotron, but is fully resolved with SFX. The study paves the way for time-resolved structural investigations of the phytochrome photocycle with time-resolved SFX.
ContributorsEdlund, Petra (Author) / Takala, Heikki (Author) / Claesson, Elin (Author) / Henry, Leocadie (Author) / Dods, Robert (Author) / Lehtivuori, Heli (Author) / Panman, Matthijs (Author) / Pande, Kanupriya (Author) / White, Thomas (Author) / Nakane, Takanori (Author) / Berntsson, Oskar (Author) / Gustavsson, Emil (Author) / Bath, Petra (Author) / Modi, Vaibhav (Author) / Roy Chowdhury, Shatabdi (Author) / Zook, James (Author) / Berntsen, Peter (Author) / Pandey, Suraj (Author) / Poudyal, Ishwor (Author) / Tenboer, Jason (Author) / Kupitz, Christopher (Author) / Barty, Anton (Author) / Fromme, Petra (Author) / Koralek, Jake D. (Author) / Tanaka, Tomoyuki (Author) / Spence, John (Author) / Liang, Mengning (Author) / Hunter, Mark S. (Author) / Boutet, Sebastien (Author) / Nango, Eriko (Author) / Moffat, Keith (Author) / Groenhof, Gerrit (Author) / Ihalainen, Janne (Author) / Stojkovic, Emina A. (Author) / Schmidt, Marius (Author) / Westenhoff, Sebastian (Author) / College of Liberal Arts and Sciences (Contributor) / School of Molecular Sciences (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / Department of Physics (Contributor)
Created2016-10-19
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Description
Serial femtosecond crystallography (SFX) using X-ray free-electron laser sources is an emerging method with considerable potential for time-resolved pump-probe experiments. Here we present a lipidic cubic phase SFX structure of the light-driven proton pump bacteriorhodopsin (bR) to 2.3 Å resolution and a method to investigate protein dynamics with modest sample requirement.

Serial femtosecond crystallography (SFX) using X-ray free-electron laser sources is an emerging method with considerable potential for time-resolved pump-probe experiments. Here we present a lipidic cubic phase SFX structure of the light-driven proton pump bacteriorhodopsin (bR) to 2.3 Å resolution and a method to investigate protein dynamics with modest sample requirement. Time-resolved SFX (TR-SFX) with a pump-probe delay of 1 ms yields difference Fourier maps compatible with the dark to M state transition of bR. Importantly, the method is very sample efficient and reduces sample consumption to about 1 mg per collected time point. Accumulation of M intermediate within the crystal lattice is confirmed by time-resolved visible absorption spectroscopy. This study provides an important step towards characterizing the complete photocycle dynamics of retinal proteins and demonstrates the feasibility of a sample efficient viscous medium jet for TR-SFX.
ContributorsNogly, Przemyslaw (Author) / Panneels, Valerie (Author) / Nelson, Garrett (Author) / Gati, Cornelius (Author) / Kimura, Tetsunari (Author) / Milne, Christopher (Author) / Milathianaki, Despina (Author) / Kubo, Minoru (Author) / Wu, Wenting (Author) / Conrad, Chelsie (Author) / Coe, Jesse (Author) / Bean, Richard (Author) / Zhao, Yun (Author) / Bath, Petra (Author) / Dods, Robert (Author) / Harimoorthy, Rajiv (Author) / Beyerlein, Kenneth R. (Author) / Rheinberger, Jan (Author) / James, Daniel (Author) / Deponte, Daniel (Author) / Li, Chufeng (Author) / Sala, Leonardo (Author) / Williams, Garth J. (Author) / Hunter, Mark S. (Author) / Koglin, Jason E. (Author) / Berntsen, Peter (Author) / Nango, Eriko (Author) / Iwata, So (Author) / Chapman, Henry N. (Author) / Fromme, Petra (Author) / Frank, Matthias (Author) / Abela, Rafael (Author) / Boutet, Sebastien (Author) / Barty, Anton (Author) / White, Thomas A. (Author) / Weierstall, Uwe (Author) / Spence, John (Author) / Neutze, Richard (Author) / Schertler, Gebhard (Author) / Standfuss, Jorg (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor) / Department of Chemistry and Biochemistry (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / School of Molecular Sciences (Contributor)
Created2016-08-22
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Description

Serial femtosecond crystallography requires reliable and efficient delivery of fresh crystals across the beam of an X-ray free-electron laser over the course of an experiment. We introduce a double-flow focusing nozzle to meet this challenge, with significantly reduced sample consumption, while improving jet stability over previous generations of nozzles. We

Serial femtosecond crystallography requires reliable and efficient delivery of fresh crystals across the beam of an X-ray free-electron laser over the course of an experiment. We introduce a double-flow focusing nozzle to meet this challenge, with significantly reduced sample consumption, while improving jet stability over previous generations of nozzles. We demonstrate its use to determine the first room-temperature structure of RNA polymerase II at high resolution, revealing new structural details. Moreover, the double flow-focusing nozzles were successfully tested with three other protein samples and the first room temperature structure of an extradiol ring-cleaving dioxygenase was solved by utilizing the improved operation and characteristics of these devices.

ContributorsOberthuer, Dominik (Author) / Knoska, Juraj (Author) / Wiedorn, Max O. (Author) / Beyerlein, Kenneth R. (Author) / Bushnell, David A. (Author) / Kovaleva, Elena G. (Author) / Heymann, Michael (Author) / Gumprecht, Lars (Author) / Kirian, Richard (Author) / Barty, Anton (Author) / Mariani, Valerio (Author) / Tolstikova, Aleksandra (Author) / Adriano, Luigi (Author) / Awel, Salah (Author) / Barthelmess, Miriam (Author) / Dorner, Katerina (Author) / Xavier, P. Lourdu (Author) / Yefanov, Oleksandr (Author) / James, Daniel (Author) / Nelson, Garrett (Author) / Wang, Dingjie (Author) / Calvey, George (Author) / Chen, Yujie (Author) / Schmidt, Andrea (Author) / Szczepek, Michael (Author) / Frielingsdorf, Stefan (Author) / Lenz, Oliver (Author) / Snell, Edward (Author) / Robinson, Philip J. (Author) / Sarler, Bozidar (Author) / Belsak, Grega (Author) / Macek, Marjan (Author) / Wilde, Fabian (Author) / Aquila, Andrew (Author) / Boutet, Sebastien (Author) / Liang, Mengning (Author) / Hunter, Mark S. (Author) / Scheerer, Patrick (Author) / Lipscomb, John D. (Author) / Weierstall, Uwe (Author) / Kornberg, Roger D. (Author) / Spence, John (Author) / Pollack, Lois (Author) / Chapman, Henry N. (Author) / Bajt, Sasa (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor)
Created2017-03-16
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Description

‘Describing at Large Their True and Lively Figure, their several Names, Conditions, Kinds, Virtues (both Natural and Fanciful), Countries of their Species, their Love and Hatred to Humankind, and the wonderful work of Natural Selection in their Evolution, Preservation, and Destruction.

Interwoven with curious variety of Creative Narrations out of Academic

‘Describing at Large Their True and Lively Figure, their several Names, Conditions, Kinds, Virtues (both Natural and Fanciful), Countries of their Species, their Love and Hatred to Humankind, and the wonderful work of Natural Selection in their Evolution, Preservation, and Destruction.

Interwoven with curious variety of Creative Narrations out of Academic Literatures, Scholars, Artists, Scientists, and Poets. Illustrated with diverse Graphics and Emblems both pleasant and profitable for Students of all Faculties and Professions.’

ContributorsHinde, Katie (Author) / Amorim, Carlos Eduardo G (Author) / Anderson, Chris (Author) / Armstrong, Ellie (Author) / Beasley, Melanie (Author) / Brokaw, Alyson F (Author) / Brubaker-Wittman, Laura (Author) / Brunstrum, Jeff (Author) / Burt, Nicole M (Author) / Casillas, Mary C (Author) / Chen, Albert (Author) / Chestnut, Tara (Author) / Coffman, Robin (Author) / Connors, Patrice K. (Author) / Dasari, Mauna (Author) / Dietrick, Jeanne (Author) / Ditelberg, Connor Fox (Author) / Drew, Josh (Author) / Durgavich, Lara (Author) / Easterling, Brian (Author) / Faust, Kaitlyn (Author) / Gabrys, Jennifer (Author) / Haridy, Yara (Author) / Hecht, Ian (Author) / Henning, Charon (Author) / Hilborn, Anne W. (Author) / Janz, Margaret (Author) / Josefson, Chloe (Author) / Karlsson, Elinor K (Author) / Kauffman, Laurie (Author) / Kissel, Jenna (Author) / Kissel, Marc (Author) / Kobylecky, Jennifer (Author) / Krell, Jason (Author) / Lee, Danielle N. (Author) / Lesciotto, Kate M (Author) / Lewton, Kristi L (Author) / Light, Jessica (Author) / Martin, Jessica Leigh, 1991- (Author) / Moore, Rick (Author) / Murphy, Asia (Author) / Murphy, Kaitlyn (Author) / Nickley, William (Author) / Nuñez-de la Mora, Alejandra (Author) / Pellicer, Olivia (Author) / Pellicer, Valeria (Author) / Perry, Anali Maughan (Author) / Popescu, Jessica (Author) / Rocha, Emily (Author) / Rubio-Godoy, Miguel (Author) / Rudzis, Cyn (Author) / Sarma, Mallika (Author) / Schuttler, Stephanie (Author) / Sinnott, Madeline (Author) / Stone, Anne C. (Author) / Tanis, Brian   (Author) / Thacher, Abbie (Author) / Upham, Nathan (Author) / Varner, Jo (Author) / Villanea, Fernando (Author) / Weber, Jesse (Author) / Wilson, Melissa A. (Author) / Willcocks, Emma (Author) / Wrensford, Kwasi (Author)
Created2023-11-06
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Description

‘Describing at Large Their True and Lively Figure, their several Names, Conditions, Kinds, Virtues (both Natural and Fanciful), Countries of their Species, their Love and Hatred to Humankind, and the wonderful work of Natural Selection in their Evolution, Preservation, and Destruction.

Interwoven with curious variety of Creative Narrations out of Academic

‘Describing at Large Their True and Lively Figure, their several Names, Conditions, Kinds, Virtues (both Natural and Fanciful), Countries of their Species, their Love and Hatred to Humankind, and the wonderful work of Natural Selection in their Evolution, Preservation, and Destruction.

Interwoven with curious variety of Creative Narrations out of Academic Literatures, Scholars, Artists, Scientists, and Poets. Illustrated with diverse Graphics and Emblems both pleasant and profitable for Students of all Faculties and Professions.’

ContributorsHinde, Katie (Author) / Amorim, Carlos Eduardo G (Author) / Anderson, Chris (Author) / Beasley, Melanie (Author) / Brokaw, Alyson F (Author) / Brubaker-Wittman, Laura (Author) / Brunstrum, Jeff (Author) / Burt, Nicole M (Author) / Casillas, Mary C (Author) / Chen, Albert (Author) / Chestnut, Tara (Author) / Coffman, Robin (Author) / Connors, Patrice K. (Author) / Dasari, Mauna (Author) / Dietrick, Jeanne (Author) / Ditelberg, Connor Fox (Author) / Drew, Josh (Author) / Durgavich, Lara (Author) / Easterling, Brian (Author) / Faust, Kaitlyn (Author) / Gabrys, Jennifer (Author) / Haridy, Yara (Author) / Hecht, Ian (Author) / Henning, Charon (Author) / Hilborn, Anne W. (Author) / Janz, Margaret (Author) / Karlsson, Elinor K (Author) / Kissel, Jenna (Author) / Kissel, Marc (Author) / Kobylecky, Jennifer (Author) / Krell, Jason (Author) / Lee, Danielle N. (Author) / Lesciotto, Kate M (Author) / Lewton, Kristi L (Author) / Light, Jessica (Author) / Martin, Jessica Leigh, 1991- (Author) / Moore, Rick (Author) / Murphy, Asia (Author) / Nickley, William (Author) / Nuñez-de la Mora, Alejandra (Author) / Pellicer, Olivia (Author) / Pellicer, Valeria (Author) / Perry, Anali Maughan (Author) / Rudzis, Cyn (Author) / Schuttler, Stephanie (Author) / Sinnott, Madeline (Author) / Stone, Anne C (Author) / Tanis, Brian   (Author) / Upham, Nathan (Author) / Villanea, Fernando (Author) / Weber, Jesse (Author) / Wilson, Melissa A. (Author) / Willcocks, Emma (Author) / Wrensford, Kwasi (Author)
Created2023-02-01
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Description

‘Describing at Large Their True and Lively Figure, their several Names, Conditions, Kinds, Virtues (both Natural and Fanciful), Countries of their Species, their Love and Hatred to Humankind, and the wonderful work of Natural Selection in their Evolution, Preservation, and Destruction.

Interwoven with curious variety of Creative Narrations out of Academic

‘Describing at Large Their True and Lively Figure, their several Names, Conditions, Kinds, Virtues (both Natural and Fanciful), Countries of their Species, their Love and Hatred to Humankind, and the wonderful work of Natural Selection in their Evolution, Preservation, and Destruction.

Interwoven with curious variety of Creative Narrations out of Academic Literatures, Scholars, Artists, Scientists, and Poets. Illustrated with diverse Graphics and Emblems both pleasant and profitable for Students of all Faculties and Professions.’

ContributorsHinde, Katie (Author) / Amorim, Carlos Eduardo G (Author) / Anderson, Chris (Author) / Andreasen, Gretchen (Author) / Armstrong, Ellie (Author) / Beasley, Melanie (Author) / Brokaw, Alyson F (Author) / Brubaker-Wittman, Laura (Author) / Brunstrum, Jeff (Author) / Burt, Nicole M (Author) / Casillas, Mary C (Author) / Chen, Albert (Author) / Chestnut, Tara (Author) / Coffman, Robin (Author) / Connors, Patrice K. (Author) / Costantini, Anthony (Author) / Dasari, Mauna (Author) / Dietrick, Jeanne (Author) / Ditelberg, Connor Fox (Author) / Drew, Josh (Author) / Durgavich, Lara (Author) / Easterling, Brian (Author) / Faust, Kaitlyn (Author) / Fogel, Arielle (Author) / Gabrys, Jennifer (Author) / Haridy, Yara (Author) / Hecht, Ian (Author) / Henning, Charon (Author) / Hilborn, Anne W. (Author) / Janz, Margaret (Author) / Josefson, Chloe (Author) / Karlsson, Elinor K (Author) / Kauffman, Laurie (Author) / Kissel, Jenna (Author) / Kissel, Marc (Author) / Kobylecky, Jennifer (Author) / Krell, Jason (Author) / Lee, Danielle N. (Author) / Lesciotto, Kate M (Author) / Lewton, Kristi L (Author) / Light, Jessica (Author) / Martin, Jessica Leigh, 1991- (Author) / Moore, Rick (Author) / Moreira, Lucas R (Author) / Murphy, Asia (Author) / Murphy, Kaitlyn (Author) / Nickley, William (Author) / Nuñez-de la Mora, Alejandra (Author) / Pellicer, Olivia (Author) / Pellicer, Valeria (Author) / Perry, Anali Maughan (Author) / Popescu, Jessica (Author) / Rocha, Emily (Author) / Rubio-Godoy, Miguel (Author) / Rudzis, Cyn (Author) / Sarma, Mallika (Author) / Schuttler, Stephanie (Author) / Sinnott, Madeline (Author) / Stone, Anne C. (Author) / Tanis, Brian   (Author) / Thacher, Abbie (Author) / Upham, Nathan (Author) / Varner, Jo (Author) / Villanea, Fernando (Author) / Weber, Jesse (Author) / Wilson, Melissa A. (Author) / Willcocks, Emma (Author) / Wrenford, Kwasi (Author) / Yates, William (Author)
Created2024-09-27
Education and Outreach: March Mammal Madness and the power of narrative in science outreach
Description

March Mammal Madness is a science outreach project that, over the course of several weeks in March, reaches hundreds of thousands of people in the United States every year. We combine four approaches to science outreach – gamification, social media platforms, community event(s), and creative products – to run a

March Mammal Madness is a science outreach project that, over the course of several weeks in March, reaches hundreds of thousands of people in the United States every year. We combine four approaches to science outreach – gamification, social media platforms, community event(s), and creative products – to run a simulated tournament in which 64 animals compete to become the tournament champion. While the encounters between the animals are hypothetical, the outcomes rely on empirical evidence from the scientific literature. Players select their favored combatants beforehand, and during the tournament scientists translate the academic literature into gripping “play-by-play” narration on social media. To date ~1100 scholarly works, covering almost 400 taxa, have been transformed into science stories. March Mammal Madness is most typically used by high-school educators teaching life sciences, and we estimate that our materials reached ~1% of high-school students in the United States in 2019. Here we document the intentional design, public engagement, and magnitude of reach of the project. We further explain how human psychological and cognitive adaptations for shared experiences, social learning, narrative, and imagery contribute to the widespread use of March Mammal Madness.

ContributorsHinde, Katie (Author) / Amorim, Carlos Eduardo G (Author) / Brokaw, Alyson F (Author) / Burt, Nicole M (Author) / Casillas, Mary C (Author) / Chen, Albert (Author) / Chestnut, Tara (Author) / Connors, Patrice K. (Author) / Dasari, Mauna (Author) / Ditelberg, Connor Fox (Author) / Dietrick, Jeanne (Author) / Drew, Josh (Author) / Durgavich, Lara (Author) / Easterling, Brian (Author) / Henning, Charon (Author) / Hilborn, Anne W. (Author) / Karlsson, Elinor K (Author) / Kissel, Marc (Author) / Kobylecky, Jennifer (Author) / Krell, Jason (Author) / Lee, Danielle N. (Author) / Lesciotto, Kate M (Author) / Lewton, Kristi L (Author) / Light, Jessica (Author) / Martin, Jessica Leigh, 1991- (Author) / Murphy, Asia (Author) / Nickley, William (Author) / Nuñez-de la Mora, Alejandra (Author) / Pellicer, Olivia (Author) / Pellicer, Valeria (Author) / Perry, Anali Maughan (Author) / Schuttler, Stephanie (Author) / Stone, Anne C (Author) / Tanis, Brian   (Author) / Weber, Jesse (Author) / Wilson, Melissa A. (Author) / Willcocks, Emma (Author) / Anderson, Chris (Author)
Created2021-02-22
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Description

X-ray free electron lasers are used in measuring diffraction patterns from nanocrystals in the 'diffract-before-destroy' mode by outrunning radiation damage. The finite-sized nanocrystals provide an opportunity to recover intensity between Bragg spots by removing the modulating function that depends on crystal shape, i.e. the transform of the crystal shape. This

X-ray free electron lasers are used in measuring diffraction patterns from nanocrystals in the 'diffract-before-destroy' mode by outrunning radiation damage. The finite-sized nanocrystals provide an opportunity to recover intensity between Bragg spots by removing the modulating function that depends on crystal shape, i.e. the transform of the crystal shape. This shape-transform dividing-out scheme for solving the phase problem has been tested using simulated examples with cubic crystals. It provides a phasing method which does not require atomic resolution data, chemical modification to the sample, or modelling based on the protein databases. It is common to find multiple structural units (e.g. molecules, in symmetry-related positions) within a single unit cell, therefore incomplete unit cells (e.g. one additional molecule) can be observed at surface layers of crystals. In this work, the effects of such incomplete unit cells on the 'dividing-out' phasing algorithm are investigated using 2D crystals within the projection approximation. It is found that the incomplete unit cells do not hinder the recovery of the scattering pattern from a single unit cell (after dividing out the shape transforms from data merged from many nanocrystals of different sizes), assuming that certain unit-cell types are preferred. The results also suggest that the dynamic range of the data is a critical issue to be resolved in order to apply the shape transform method practically.

ContributorsLiu, Haiguang (Author) / Zatsepin, Nadia (Author) / Spence, John (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor)
Created2014-01-01