scholarly journals Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

10.3791/57133 ◽  
2018 ◽  
Author(s):  
Yannig Gicquel ◽  
Robin Schubert ◽  
Svetlana Kapis ◽  
Gleb Bourenkov ◽  
Thomas Schneider ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Microfluidic Chips ◽  
X Ray Diffraction ◽  
X Ray ◽  
Serial Crystallography

Dynamic Light Scattering at CdSe Nanocrystals and CdSe Cluster-Molecules

2000 ◽  
Vol 636 ◽  
Author(s):  
A. Eichhöfer ◽  
C.V. Hänisch ◽  
M. Jacobsohn ◽  
U. Banin
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
High Performance ◽  
Size Range ◽  
Blue Shift ◽  
Cdse Nanocrystals ◽  
Particle Sizes ◽  
X Ray Diffraction ◽  
X Ray

AbstractHigh performance dynamic light scattering (DLS) has been used to determine the hydrodynamic diameters of CdSe-nanocrystals as well as CdSe cluster molecules in a size range of 1 to 10 nm. The method enables the determination of the particle sizes including the ligand shells directly in solution. Consistent with the blue shift of the absorption onset by reducing the particle sizes the values for the hydrodynamic radii decrease. For the CdSe nanoparticles the measured sizes were compared with the diameters determined by TEM experiments; the sizes of the cluster molecules were on the other hand estimated from the space filling models of the single crystal X-ray structure determination. Regarding both types of compounds, DLS yield comparable values for the radii, indicating that it provides a potentially important tool in addition to other size determining techniques like TEM, which operates at more drastic conditions, and powder X-ray diffraction being difficult to interpret below 5 nm.

scholarly journals An automated platform for in situ serial crystallography at room temperature

IUCrJ ◽  
2020 ◽  
Vol 7 (6) ◽  
pp. 1009-1018
Author(s):  
Zhong Ren ◽  
Cong Wang ◽  
Heewhan Shin ◽  
Sepalika Bandara ◽  
Indika Kumarapperuma ◽  
...  
Keyword(s):  
Data Collection ◽  
Room Temperature ◽  
Protein Structures ◽  
Routine Data ◽  
Protein Crystals ◽  
X Ray Diffraction ◽  
X Ray ◽  
Serial Crystallography ◽  
Routine Data Collection

Direct observation of functional motions in protein structures is highly desirable for understanding how these nanomachineries of life operate at the molecular level. Because cryogenic temperatures are non-physiological and may prohibit or even alter protein structural dynamics, it is necessary to develop robust X-ray diffraction methods that enable routine data collection at room temperature. We recently reported a crystal-on-crystal device to facilitate in situ diffraction of protein crystals at room temperature devoid of any sample manipulation. Here an automated serial crystallography platform based on this crystal-on-crystal technology is presented. A hardware and software prototype has been implemented, and protocols have been established that allow users to image, recognize and rank hundreds to thousands of protein crystals grown on a chip in optical scanning mode prior to serial introduction of these crystals to an X-ray beam in a programmable and high-throughput manner. This platform has been tested extensively using fragile protein crystals. We demonstrate that with affordable sample consumption, this in situ serial crystallography technology could give rise to room-temperature protein structures of higher resolution and superior map quality for those protein crystals that encounter difficulties during freezing. This serial data collection platform is compatible with both monochromatic oscillation and Laue methods for X-ray diffraction and presents a widely applicable approach for static and dynamic crystallographic studies at room temperature.

scholarly journals Monitoring the Production of High Diffraction-Quality Crystals of Two Enzymes in Real Time Using In Situ Dynamic Light Scattering

Crystals ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 65
Author(s):  
Raphaël de Wijn ◽  
Kévin Rollet ◽  
Sylvain Engilberge ◽  
Alastair G. McEwen ◽  
Oliver Hennig ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Growth Conditions ◽  
Psychrophilic Bacterium ◽  
X Ray Diffraction ◽  
Crystallization System ◽  
Rational Production ◽  
Hen Egg White ◽  
High Diffraction

The reproducible preparation of well-diffracting crystals is a prerequisite for every structural study based on crystallography. An instrument called XtalController has recently been designed that allows the monitoring of crystallization assays using dynamic light scattering and microscopy, and integrates piezo pumps to alter the composition of the mother liquor during the experiment. We have applied this technology to study the crystallization of two enzymes, the CCA-adding enzyme of the psychrophilic bacterium Planococcus halocryophilus, and the lysozyme from hen egg white in the presence of a synthetic chemical nucleant. We were able to (i) detect early nucleation events and (ii) drive the crystallization system (through cycles of dissolution/crystallization) toward growth conditions yielding crystals with excellent diffraction properties. This technology opens a way to the rational production of samples for crystallography, ranging from nanocrystals for electron diffraction, microcrystals for serial or conventional X-ray diffraction, to larger crystals for neutron diffraction.

scholarly journals Monitoring the production of high diffraction-quality crystals of two enzymes in real time using in situ dynamic light scattering

2020 ◽  
Author(s):  
Raphaël de Wijn ◽  
Kévin Rollet ◽  
Sylvain Engilberge ◽  
Alastair G. McEwen ◽  
Oliver Hennig ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Growth Conditions ◽  
Psychrophilic Bacterium ◽  
X Ray Diffraction ◽  
Egg White Lysozyme ◽  
Crystallization System ◽  
Rational Production ◽  
Hen Egg White

ABSTRACTThe reproducible preparation of well diffracting crystals is a prerequisite for every structural study based on crystallography. An instrument called the XtalController has recently been designed that allows the monitoring of crystallization assays using dynamic light scattering and microscopy, and integrates piezo pumps to alter the composition of the mother liquor during the experiment. We have applied this technology to study the crystallization of two enzymes, the CCA-adding enzyme of the psychrophilic bacterium Planococcus halocryophilus and the hen egg white lysozyme in the presence of a synthetic chemical nucleant. We were able to i) detect early nucleation events and ii) drive the crystallization system (through cycles of dissolution/crystallization) towards growth conditions yielding crystals with excellent diffraction properties. This technology opens a way to the rational production of samples for crystallography, ranging from nanocrystals for electron diffraction, microcrystals for serial or conventional X-ray diffraction, to larger crystals for neutron diffraction.

scholarly journals Coprecipitation Method of Synthesis, Characterization, and Cytotoxicity of Pr3+:LaF3 (CPr = 3, 7, 12, 20, 30%) Nanoparticles

2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Maksim S. Pudovkin ◽  
Pavel V. Zelenikhin ◽  
Victoria Shtyreva ◽  
Oleg A. Morozov ◽  
Darya A. Koryakovtseva ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Light Scattering ◽  
High Resolution ◽  
Dynamic Light Scattering ◽  
Hydrodynamic Radius ◽  
Average Diameter ◽  
X Ray Diffraction ◽  
X Ray ◽  
Transmission Electron

The Pr3+:LaF3 (CPr = 3, 7, 12, 20, 30%) nanoparticles were characterized by means of high-resolution transmission electron microscopy, X-ray diffraction, optical spectroscopy, energy dispersive X-ray spectroscopy, dynamic light scattering, and MTT assay. It was revealed that the average diameter of all the NPs is around 14–18 nm. The hydrodynamic radius of the Pr3+:LaF3 (CPr = 7%) nanoparticles strongly depends on the medium. It was revealed that hydrodynamic radii of the Pr3+:LaF3 (CPr = 7%) nanoparticles in water, DMEM, and RPMI-1640 biological mediums were 18 ± 5, 41 ± 6, and 186 ± 8 nm, respectively. The Pr3+:LaF3 (CPr = 7%) nanoparticles were nontoxic at micromolar concentrations toward COLO-320 cell line. The lifetime curves were fitted biexponentially, and for the Pr3+:LaF3 (CPr = 7%) NPs, the luminescence lifetimes of Pr3+ ions were 480 ± 2 and 53 ± 5 nanosec.

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