ASU in Hollywood brings top executives to class

December 5, 2014

Aspiring stars of stage and screen have tried many things to get their shot at fame and fortune. But one Arizona State University alumnus who has made it to the top of Hollywood has simple advice: hard work and dedication can get you where you want to go.

“Find something that you love and stick to it,” said Michael Burns, the vice chairman of Lionsgate, speaking to an ASU film class this week in Santa Monica, California. “Devote time to it.” students watching live feed projection of person speaking ASU film and media students on the Tempe campus listen to Michael Burns, vice chairman of Lionsgate, speak during a live feed of a "Welcome to Hollywood" class at ASU's California Center in Santa Monica. Download Full Image

Burns shared his experiences, some life lessons and personal advice on how to make it in a notoriously competitive industry at the “Welcome to Hollywood” class taught at ASU’s California Center by film professor Adam Collis.

He argued that, along with dedication, the ambition to strive for big things is crucial to being able to achieve them.

“When looking for a job, you have to ask yourself, where would you be great?” he said. “And then dare to be great.”

Burns has close ties to ASU, where he studied political science and was the president of his fraternity. Now he is the leader of Lionsgate’s corporate management team, and has been involved in the acquisition and production of some of Lionsgate’s biggest box office hits.

The “Welcome to Hollywood” course is part of ASU in Hollywood, a collection of ad hoc classes, programs and internships run by Collis, a professor in the School of Film, Dance and Theatre in the Herberger Institute for Design and the Arts. The goals of "Welcome to Hollywood" include broadening ASU students’ exposure to leaders in the film and television industry. The program also aims to connect ASU to California’s biggest metropolitan area.

In fact, Burns’ speech was streamed live onto the Tempe campus, where 20 Arizona-based students had the opportunity to participate in and interact with the class.

Steven Wallace, an ASU grad who attended the lecture on the California side, said he learned details about budgeting and foreign affairs from Burns’s talk, in addition to getting to hear his words of wisdom.

“He was a very personable speaker, and I just liked his overall message,” Wallace said.

One of those messages was that new technologies can create openings for new opportunities in storytelling.

“You want to go where the puck is going,” Burns told students. “You don’t want to go where it’s been.”

Lionsgate was ahead of the media curve when it came to technology, Burns said, but around the globe technology continues to grow.

Burns is also a believer in social media and argues YouTube can be harnessed to increase someone’s profile: the perfect tool to broadcast uniqueness and get a name noticed.

While Burns touched on the technical and corporate side of the entertainment business, he said he shared his experiences to prove that people have to dig deep in order to survive in this industry.

“Everyone has something unique about themselves. Everyone has a hook. Make yourself stand out,” he said.

Written by Jillian Lopez

New research paves the way for nano-movies of biomolecules

December 5, 2014

An international team, including scientists from Arizona State University, the University of Wisconsin-Milwaukee (UWM) and Germany’s Deutsches Elektronen-Synchrotron (DESY), have caught a light sensitive biomolecule at work using an X-ray laser. Their new study proves that high-speed X-ray lasers can capture the fast dynamics of biomolecules in ultra slow-motion, revealing subtle processes with unprecedented clarity.

"This work paves the way for movies from the nano-world with atomic resolution," said professor Marius Schmidt from UWM, corresponding author of the new paper, which appears in the Dec. 4 issue of the journal Science. ray of light Download Full Image

Study co-author Petra Fromme, a professor in ASU’s Department of Chemistry and Biochemistry, echoes the importance of the new study: “This paper is very exciting, as it is the first report of time-resolved studies with serial femtosecond crystallography that unravels details at atomic resolution,” said Fromme. “This is a huge breakthrough toward the ultimate goal of producing molecular movies that reveal the dynamics of biomolecules with unparalleled speed and precision.”

A femtosecond is a quadrillionth of a second, an almost unfathomably brief duration. Around 100 femtoseconds are required for a ray of light to traverse the width of a human hair.

The technique of X-ray crystallography allows researchers to probe atomic and molecular structure, by exposing crystals to incident X-rays that diffract from the sample in various directions. Careful measurement of X-ray diffraction angles and intensities allows a three-dimensional portrait of electron densities to be constructed – information used to define atomic structure.

The technique has been an invaluable tool for investigating the structure and function of a broad range of biologically important molecules, including drugs, vitamins, proteins and nucleic acids like DNA.

But just as shutter speed determines a camera’s ability to capture action of very short duration, so X-ray lasers must deliver extremely brief pulses of light to capture fine structure and dynamic processes at the atomic level. Some of the phenomena researchers wish to explore take place in mere quadrillionths of a second. A new generation of ultrafast lasers, like the Linac Coherent Light Source (LCLS) at SLAC National Accelerator Laboratory (used in the current study), are redefining the field of X-ray crystallography.

The researchers used the photoactive yellow protein (PYP) as a model system. PYP is a receptor for blue light that is part of the photosynthetic machinery in certain bacteria. When it catches a blue photon, it cycles through various intermediate structures as it harvests the energy of the photon, before returning to its initial state. Most steps of this PYP photocycle have been well-studied, making it an excellent candidate for validating a new method.

For their ultrafast snapshots of PYP dynamics, the scientists first produced tiny crystals of PYP molecules, most measuring less than 0.01 millimeters across. The dynamics of these microcrystals were captured in exquisite detail when the world’s most powerful X-ray laser at SLAC was trained on them. Initiation of their photocycle was triggered with a precisely synchronised blue laser pulse.

Thanks to the incredibly short and intense X-ray flashes of the LCLS, the researchers could observe different steps in the PYP photocycle with a resolution of 0.16 nanometers, by taking snapshots of X-ray diffraction patterns. The spectacular time resolution afforded by the technique allows researchers to detect changes in the atomic-scale conformation of PYP molecules as they switch back and forth between light and dark states.

The investigation not only reproduced what was already known about the PYP photocycle, thereby validating the new method, it also imaged delicate phenomena in much finer detail. Thanks to the high temporal resolution, the X-ray laser could in principle study steps in the cycle that are shorter than 1 picosecond (a trillionth of a second) – too fast to be captured with previous techniques. The ultrafast snapshots can be assembled into a movie, detailing the dynamics in ultra slow-motion.

“This is far more than a proof of concept for time-resolved crystallography. LCLS can use micron size crystals and therefore have an unmatched light initiation efficiency to explore uncharted territory in the dimension of time resolution of molecular reactions,” Raimund Fromme stated, an ASU associate research professor participating in this project.

"This is a real breakthrough," emphasizes co-author professor Henry Chapman from DESY. "Our study is opening the door for time-resolved studies of dynamic processes, providing an unprecedented window on subtle transformations at the atomic scale."

John Spence, director of science for the Science and Technology Center at ASU, stresses the importance of studying delicate life processes by means of new tools capable of extreme spatial and temporal resolution:

"When combined with previous work, it is remarkable now to be able to assemble a true molecular movie of the photocycle of this blue light detector in bacteria at atomic resolution, with the intermediate structures appearing and fading in the correct sequence. It is a huge step forward, which will also aid research on artificial photosynthesis,” he says. “It builds on our earlier work at LCLS, and is supported by our NSF Science and Technology Center for the use of X-ray lasers in biology."

The new research is built on the first time-resolved serial femstosecond crystallography studies on a protein, Photosystem II, that was led by the team of researchers at ASU. The study on PYP now shows that time-resolved crystallography can unravel details of the dynamics of a protein at the atomic level.

The ASU team involved in this study includes four faculty and their research teams (John Spence, Uwe Weierstall, Petra Fromme and Raimund Fromme) from the Departments of Physics and Chemistry and Biochemistry who are members of the new Center for Applied Structural Discovery at the Biodesign Institute. The ASU team contributed to many aspects of the study, which range from experimental planning to the application of injector technology, growth and biophysical characterization of the PYP microcrystals and data evaluation.

The ASU team also includes the graduate students Christopher Kupitz, Chelsie Conrad, Jesse Coe, Shatabdi Roy-Chowdhury, who worked on the growth and biophysical characterization of the PYP crystals at ASU and on-site at LCLS, the graduate students Daniel James and Dingjie Wang, who worked on sample delivery, as well as the research scientist Nadia Zatsepin and the graduate student Shibom Basu, who worked on “on-the-fly” data evaluation.

“Since the sample injector developed at ASU allows for continuous sample replenishment, the X-ray laser always probes fresh, undamaged crystals, allowing us to make molecular movies of irreversible reactions,” says research professor Uwe Weierstall. Further, X-ray lasers typically investigate very small crystals that often are much easier to fabricate than larger crystals. In fact, some biomolecules are so hard to crystallise that they can only be investigated with an X-ray laser.

“This is the highest resolution X-ray laser dataset we’ve worked with – these tiny crystals were of very high quality,” adds research scientist Nadia Zatsepin. “It was very satisfying to see such high resolution electron densities by the second day of our experiment, but to then also see such strong signals from the changes in the structure was even more exciting.”

The small crystal size is also an advantage when it comes to kick-starting molecular dynamics uniformly across the sample. In larger samples, the initiating optical laser pulse is often quickly absorbed in the sample, which excites only a thin layer and leaves the bulk of the crystal unaffected.

The PYP microcrystals were perfectly matched to the optical absorption so that the entire crystal was undergoing dynamics, which in turn allows sensitive measurements of the molecular changes by snapshot X-ray diffraction.

Taken together, X-ray laser investigations can offer previously inaccessible insights into the dynamics of the molecular world, complementing other methods. Using the ultra slow-motion, the scientists next plan to elucidate the fast steps of the PYP photocycle that are too short to be seen with previous methods.

In the future, ultrafast laser crystallography promises to illuminate a broad range of biomolecules, from light sensitive photoreceptors to other vital proteins.

Richard Harth

Science writer, Biodesign Institute at ASU