Matching Items (12)
Description
Single particle diffractive imaging data from Rice Dwarf Virus (RDV) were recorded using the Coherent X-ray Imaging (CXI) instrument at the Linac Coherent Light Source (LCLS). RDV was chosen as it is a well-characterized model system, useful for proof-of-principle experiments, system optimization and algorithm development. RDV, an icosahedral virus of about 70 nm in diameter, was aerosolized and injected into the approximately 0.1 μm diameter focused hard X-ray beam at the CXI instrument of LCLS. Diffraction patterns from RDV with signal to 5.9 Ångström were recorded. The diffraction data are available through the Coherent X-ray Imaging Data Bank (CXIDB) as a resource for algorithm development, the contents of which are described here.
ContributorsMunke, Anna (Author) / Andreasson, Jakob (Author) / Aquila, Andrew (Author) / Awel, Salah (Author) / Ayyer, Kartik (Author) / Barty, Anton (Author) / Bean, Richard J. (Author) / Berntsen, Peter (Author) / Bielecki, Johan (Author) / Boutet, Sebastien (Author) / Bucher, Maximilian (Author) / Chapman, Henry N. (Author) / Daurer, Benedikt J. (Author) / DeMirci, Hasan (Author) / Elser, Veit (Author) / Fromme, Petra (Author) / Hajdu, Janos (Author) / Hantke, Max F. (Author) / Higashiura, Akifumi (Author) / Hogue, Brenda (Author) / Hosseinizadeh, Ahmad (Author) / Kim, Yoonhee (Author) / Kirian, Richard (Author) / Reddy, Hemanth K. N. (Author) / Lan, Ti-Yen (Author) / Larsson, Daniel S. D. (Author) / Liu, Haiguang (Author) / Loh, N. Duane (Author) / Maia, Filipe R. N. C. (Author) / Mancuso, Adrian P. (Author) / Muhlig, Kerstin (Author) / Nakagawa, Atsushi (Author) / Nam, Daewoong (Author) / Nelson, Garrett (Author) / Nettelblad, Carl (Author) / Okamoto, Kenta (Author) / Ourmazd, Abbas (Author) / Rose, Max (Author) / van der Schot, Gijs (Author) / Schwander, Peter (Author) / Seibert, M. Marvin (Author) / Sellberg, Jonas A. (Author) / Sierra, Raymond G. (Author) / Song, Changyong (Author) / Svenda, Martin (Author) / Timneanu, Nicusor (Author) / Vartanyants, Ivan A. (Author) / Westphal, Daniel (Author) / Wiedom, Max O. (Author) / Williams, Garth J. (Author) / Xavier, Paulraj Lourdu (Author) / Soon, Chun Hong (Author) / Zook, James (Author) / College of Liberal Arts and Sciences (Contributor, Contributor) / School of Molecular Sciences (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / School of Life Sciences (Contributor) / Infectious Diseases and Vaccinology (Contributor) / Department of Physics (Contributor)
Created2016-08-01
Description
Background
Physical activity prevents or delays progression of impaired glucose tolerance in high-risk individuals. Physical activity promotion should serve as a basis in diabetes care. It is necessary to develop and evaluate health-promoting methods that are feasible as well as cost-effective within diabetes care. The aim of Sophia Step Study is to evaluate the impact of a multi-component and a single component physical activity intervention aiming at improving HbA[subscript 1c] (primary outcome) and other metabolic and cardiovascular risk factors, physical activity levels and overall health in patients with pre- and type 2 diabetes.
Methods/design
Sophia Step Study is a randomized controlled trial and participants are randomly assigned to either a multi-component intervention group (A), a pedometer group (B) or a control group (C). In total, 310 patients will be included and followed for 24 months. Group A participants are offered pedometers and a website to register steps, physical activity on prescription with yearly follow-ups, motivational interviewing (10 occasions) and group consultations (including walks, 12 occasions). Group B participants are offered pedometers and a website to register steps. Group C are offered usual care. The theoretical framework underpinning the interventions is the Health Belief Model, the Stages of Change Model, and the Social Cognitive Theory. Both the multi-component intervention (group A) and the pedometer intervention (group B) are using several techniques for behavior change such as self-monitoring, goal setting, feedback and relapse prevention.
Measurements are made at week 0, 8, 12, 16, month 6, 9, 12, 18 and 24, including metabolic and cardiovascular biomarkers (HbA[subscript 1c] as primary health outcome), accelerometry and daily steps. Furthermore, questionnaires were used to evaluate dietary intake, physical activity, perceived ability to perform physical activity, perceived support for being active, quality of life, anxiety, depression, well-being, perceived treatment, perceived stress and diabetes self- efficacy.
Discussion
This study will show if a multi-component intervention using pedometers with group- and individual consultations is more effective than a single- component intervention using pedometers alone, in increasing physical activity and improving HbA[subscript 1c], other metabolic and cardiovascular risk factors, physical activity levels and overall health in patients with pre- and type 2 diabetes.
Physical activity prevents or delays progression of impaired glucose tolerance in high-risk individuals. Physical activity promotion should serve as a basis in diabetes care. It is necessary to develop and evaluate health-promoting methods that are feasible as well as cost-effective within diabetes care. The aim of Sophia Step Study is to evaluate the impact of a multi-component and a single component physical activity intervention aiming at improving HbA[subscript 1c] (primary outcome) and other metabolic and cardiovascular risk factors, physical activity levels and overall health in patients with pre- and type 2 diabetes.
Methods/design
Sophia Step Study is a randomized controlled trial and participants are randomly assigned to either a multi-component intervention group (A), a pedometer group (B) or a control group (C). In total, 310 patients will be included and followed for 24 months. Group A participants are offered pedometers and a website to register steps, physical activity on prescription with yearly follow-ups, motivational interviewing (10 occasions) and group consultations (including walks, 12 occasions). Group B participants are offered pedometers and a website to register steps. Group C are offered usual care. The theoretical framework underpinning the interventions is the Health Belief Model, the Stages of Change Model, and the Social Cognitive Theory. Both the multi-component intervention (group A) and the pedometer intervention (group B) are using several techniques for behavior change such as self-monitoring, goal setting, feedback and relapse prevention.
Measurements are made at week 0, 8, 12, 16, month 6, 9, 12, 18 and 24, including metabolic and cardiovascular biomarkers (HbA[subscript 1c] as primary health outcome), accelerometry and daily steps. Furthermore, questionnaires were used to evaluate dietary intake, physical activity, perceived ability to perform physical activity, perceived support for being active, quality of life, anxiety, depression, well-being, perceived treatment, perceived stress and diabetes self- efficacy.
Discussion
This study will show if a multi-component intervention using pedometers with group- and individual consultations is more effective than a single- component intervention using pedometers alone, in increasing physical activity and improving HbA[subscript 1c], other metabolic and cardiovascular risk factors, physical activity levels and overall health in patients with pre- and type 2 diabetes.
ContributorsRossen, Jenny (Author) / Yngve, Agneta (Author) / Hagstromer, Maria (Author) / Brismar, Kerstin (Author) / Ainsworth, Barbara (Author) / Iskull, Christina (Author) / Moller, Peter (Author) / Johansson, Unn-Britt (Author) / College of Health Solutions (Contributor) / School of Nutrition and Health Promotion (Contributor)
Created2015-07-12
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
Description
The transient receptor potential channel subfamily V member 1 (TRPV1) functions as the heat and capsaicin receptor. It can be activated by heat, protons, pungent chemicals, and a variety of other endogenous mediators of nociception. TRPV1 is a non-selective cation channel consisting of 6 transmembrane domains (S1-S6), with helices S1-S4 forming the sensing domain and the S5-S6 helices forming the pore domain. Understanding the TRPV1 channel is imperative due to its relation to a variety of human diseases, including cancer, type II diabetes, hyper and hypothermia, and inflammatory disorders of the airways and bladder. Although TRPV1 is the best-studied thermosensitive-TRP channels of all the 28 family members, the molecular underpinning and the contributions of the human TRPV1 pore domain in thermo-sensing remains elusive. Recently, the human TRPV1 sensing domain was found to contribute to heat activation. It was found to undergo a non-denaturing temperature-dependent conformational change. This finding triggered interest in studying the function and the role of the human TRPV1 pore domain in the heat activation process. Specifically, to identify whether heat activation is intrinsic to the pore domain. This thesis paper explores and optimizes the purification protocol of the human TRPV1 pore domain through three different methods. The first method was using a denaturant, the second method was increasing the length of the histidine tags through Q5 insertion, and the third method was incorporating the protein construct into nanodiscs. In addition to the above three methods, size exclusion chromatography and ion-exchange chromatography were utilized after thrombin cleavage to separate the human TRPV1 pore domain from the cleaved MBP deca-histidine tags as well as the impurities.
ContributorsChang, Yu Tzu (Author) / Van Horn, Wade (Thesis director) / Wang, Xu (Committee member) / Cherry, Brian (Committee member) / School of Molecular Sciences (Contributor) / School of Life Sciences (Contributor) / Barrett, The Honors College (Contributor)
Created2020-12
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 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
Description
The entirely soft-tissue anatomy of the octopus arm provides the animal with a large amount of freedom of movement, while still allowing the specimen to support itself despite the lack of a skeletal system. This is made possible through the use of various muscle layers within the octopus arm, which act as muscular hydrostats. Magnetic Resonance imaging of the octopus arm was employed to view the muscle layers within the octopus arm and observe trends and differences in these layers at the proximal, middle, and distal portions of the arms. A total of 39 arms from 6 specimens were imaged to give 112 total imaged sections (38 proximal, 37 middle, 37 distal). Significant increases in both the internal longitudinal muscle layer and the nervous core were found between the proximal and middle, proximal and distal, and middle and distal sections of the arms. This could reflect selection for these structures distally in the octopus arm for predator or other noxious stimuli avoidance. A significant decrease in the transverse muscle layer was found in the middle and distal sections of the arms. This could reflect selection for elongation in the proximal portion of the octopus arm or could be the result of selection for the internal longitudinal muscle layer and nervous core distally. Previous studies on Octopus vulgaris showed a preference for using the proximal arms in the pushing movement of crawling and a preference for using the anterior arms in exploring behaviors (Levy et al., 2015 and Byrne et al., 2006). Differences between the anterior and posterior arms for the transverse muscle layer, internal longitudinal muscle layer, and the nervous core were insignificant, reflecting a lack of structure-function relationships. This could also be due to a low sample size. Differences between the left and right arms for the transverse muscle layer, internal longitudinal muscle layer, and the nervous core were insignificant, supporting previous evidence that left versus right eye and arm preferences in octopus are not population-wide, but individual. Some slight trends can be found for individual arms, but the sample size was too small to make definitive statements regarding differences among specific arms.
ContributorsRoy, Cayla C (Author) / Fisher, Rebecca (Thesis director) / Marvi, Hamid (Committee member) / Cherry, Brian (Committee member) / Watts College of Public Service & Community Solut (Contributor) / School of Life Sciences (Contributor) / School of Molecular Sciences (Contributor) / Barrett, The Honors College (Contributor)
Created2019-05
Description
Octopus arms employ a complex three dimensional array of musculature, called a
muscular hydrostat, which allows for nearly infinite degrees of freedom of movement without
the structure of a skeletal system. This study employed Magnetic Resonance Imaging with a
Gadoteridol-based contrast agent to image the octopus arm and view the internal tissues. Muscle
layering was mapped and area was measured using AMIRA image processing and the trends in
these layers at the proximal, middle, and distal portions of the arms were analyzed. A total of 39
arms from 6 specimens were scanned to give 112 total imaged sections (38 proximal, 37 middle,
37 distal), from which to ascertain and study the possible differences in musculature. The
images revealed significant increases in the internal longitudinal muscle layer percentages
between the proximal and middle, proximal and distal, and middle and distal sections of the
arms. These structural differences are hypothesized to be used for rapid retraction of the distal
segment when encountering predators or noxious stimuli. In contrast, a significant decrease in
the transverse muscle layer was found when comparing the same sections. These structural
differences are hypothesized to be a result of bending behaviors during retraction. Additionally,
the internal longitudinal layer was separately studied orally, toward the sucker, and aborally,
away from the sucker. The significant differences in oral and aboral internal longitudinal
musculature in proximal, middle, and distal sections is hypothesized to support the pseudo-joint
functionality displayed in octopus fetching behaviors. The results indicate that individual
octopus arm morphology is more unique than previously thought and supports that internal
structural differences exist to support behavioral functionality.
muscular hydrostat, which allows for nearly infinite degrees of freedom of movement without
the structure of a skeletal system. This study employed Magnetic Resonance Imaging with a
Gadoteridol-based contrast agent to image the octopus arm and view the internal tissues. Muscle
layering was mapped and area was measured using AMIRA image processing and the trends in
these layers at the proximal, middle, and distal portions of the arms were analyzed. A total of 39
arms from 6 specimens were scanned to give 112 total imaged sections (38 proximal, 37 middle,
37 distal), from which to ascertain and study the possible differences in musculature. The
images revealed significant increases in the internal longitudinal muscle layer percentages
between the proximal and middle, proximal and distal, and middle and distal sections of the
arms. These structural differences are hypothesized to be used for rapid retraction of the distal
segment when encountering predators or noxious stimuli. In contrast, a significant decrease in
the transverse muscle layer was found when comparing the same sections. These structural
differences are hypothesized to be a result of bending behaviors during retraction. Additionally,
the internal longitudinal layer was separately studied orally, toward the sucker, and aborally,
away from the sucker. The significant differences in oral and aboral internal longitudinal
musculature in proximal, middle, and distal sections is hypothesized to support the pseudo-joint
functionality displayed in octopus fetching behaviors. The results indicate that individual
octopus arm morphology is more unique than previously thought and supports that internal
structural differences exist to support behavioral functionality.
ContributorsCummings, Sheldon Daniel (Author) / Fisher, Rebecca (Thesis director) / Marvi, Hamidreza (Committee member) / Cherry, Brian (Committee member) / Harrington Bioengineering Program (Contributor) / Barrett, The Honors College (Contributor)
Created2019-05
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
Mix-and-inject serial crystallography (MISC) is a technique designed to image enzyme catalyzed reactions in which small protein crystals are mixed with a substrate just prior to being probed by an X-ray pulse. This approach offers several advantages over flow cell studies. It provides (i) room temperature structures at near atomic resolution, (ii) time resolution ranging from microseconds to seconds, and (iii) convenient reaction initiation. It outruns radiation damage by using femtosecond X-ray pulses allowing damage and chemistry to be separated. Here, we demonstrate that MISC is feasible at an X-ray free electron laser by studying the reaction of M. tuberculosis ß-lactamase microcrystals with ceftriaxone antibiotic solution. Electron density maps of the apo-ß-lactamase and of the ceftriaxone bound form were obtained at 2.8 Å and 2.4 Å resolution, respectively. These results pave the way to study cyclic and non-cyclic reactions and represent a new field of time-resolved structural dynamics for numerous substrate-triggered biological reactions.
ContributorsKupitz, Christopher (Author) / Olmos, Jose L. (Author) / Holl, Mark (Author) / Tremblay, Lee (Author) / Pande, Kanupriya (Author) / Pandey, Suraj (Author) / Oberthur, Dominik (Author) / Hunter, Mark (Author) / Liang, Mengning (Author) / Aquila, Andrew (Author) / Tenboer, Jason (Author) / Calvey, George (Author) / Katz, Andrea (Author) / Chen, Yujie (Author) / Wiedorn, Max O. (Author) / Knoska, Juraj (Author) / Meents, Alke (Author) / Majriani, Valerio (Author) / Norwood, Tyler (Author) / Poudyal, Ishwor (Author) / Grant, Thomas (Author) / Miller, Mitchell D. (Author) / Xu, Weijun (Author) / Tolstikova, Aleksandra (Author) / Morgan, Andrew (Author) / Metz, Markus (Author) / Martin Garcia, Jose Manuel (Author) / Zook, James (Author) / Roy Chowdhury, Shatabdi (Author) / Coe, Jesse (Author) / Nagaratnam, Nirupa (Author) / Meza-Aguilar, Domingo (Author) / Fromme, Raimund (Author) / Basu, Shibom (Author) / Frank, Matthias (Author) / White, Thomas (Author) / Barty, Anton (Author) / Bajt, Sasa (Author) / Yefanov, Oleksandr (Author) / Chapman, Henry N. (Author) / Zatsepin, Nadia (Author) / Nelson, Garrett (Author) / Weierstall, Uwe (Author) / Spence, John (Author) / Schwander, Peter (Author) / Pollack, Lois (Author) / Fromme, Petra (Author) / Ourmazd, Abbas (Author) / Phillips, George N. (Author) / Schmidt, Marius (Author) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor) / School of Molecular Sciences (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor)
Created2016-12-15
Description
Serial femtosecond crystallography (SFX) has opened a new era in crystallography by permitting nearly damage-free, room-temperature structure determination of challenging proteins such as membrane proteins. In SFX, femtosecond X-ray free-electron laser pulses produce diffraction snapshots from nanocrystals and microcrystals delivered in a liquid jet, which leads to high protein consumption. A slow-moving stream of agarose has been developed as a new crystal delivery medium for SFX. It has low background scattering, is compatible with both soluble and membrane proteins, and can deliver the protein crystals at a wide range of temperatures down to 4°C. Using this crystal-laden agarose stream, the structure of a multi-subunit complex, phycocyanin, was solved to 2.5 Å resolution using 300 µg of microcrystals embedded into the agarose medium post-crystallization. The agarose delivery method reduces protein consumption by at least 100-fold and has the potential to be used for a diverse population of proteins, including membrane protein complexes.
ContributorsConrad, Chelsie (Author) / Basu, Shibom (Author) / James, Daniel (Author) / Wang, Dingjie (Author) / Schaffer, Alexander (Author) / Roy Chowdhury, Shatabdi (Author) / Zatsepin, Nadia (Author) / Aquila, Andrew (Author) / Coe, Jesse (Author) / Gati, Cornelius (Author) / Hunter, Mark S. (Author) / Koglin, Jason E. (Author) / Kupitz, Christopher (Author) / Nelson, Garrett (Author) / Subramanian, Ganesh (Author) / White, Thomas A. (Author) / Zhao, Yun (Author) / Zook, James (Author) / Boutet, Sebastien (Author) / Cherezov, Vadim (Author) / Spence, John (Author) / Fromme, Raimund (Author) / Weierstall, Uwe (Author) / Fromme, Petra (Author) / Department of Chemistry and Biochemistry (Contributor) / Biodesign Institute (Contributor) / Applied Structural Discovery (Contributor) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor) / School of Molecular Sciences (Contributor)
Created2015-06-30