Bond Shortening (1.4 Å) in the Singlet and Triplet Excited States of [Ir2(dimen)4]2+in Solution Determined by Time-Resolved X-ray Scattering

2011 ◽  
Vol 50 (19) ◽  
pp. 9329-9336 ◽  
Author(s):  
Kristoffer Haldrup ◽  
Tobias Harlang ◽  
Morten Christensen ◽  
Asmus Dohn ◽  
Tim Brandt van Driel ◽  
...  
Keyword(s):  
Excited States ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Triplet Excited States ◽  
Ray Scattering

Analysis of time-resolved X-ray scattering data from solution-state systems

2010 ◽  
Vol 66 (2) ◽  
pp. 261-269 ◽  
Author(s):  
Kristoffer Haldrup ◽  
Morten Christensen ◽  
Martin Meedom Nielsen
Keyword(s):  
Excited States ◽  
Structural Parameters ◽  
Scattering Data ◽  
Platinum Compound ◽  
Time Resolved ◽  
X Ray ◽  
The Past ◽  
X Ray Scattering ◽  
Liquid Systems ◽  
Ray Scattering

As ultrafast time-resolved studies of liquid systems with the laser pump/X-ray scattering probe method have come of age over the past decade, several groups have developed methods for the analysis of such X-ray scattering data. The present article describes a method developed primarily with a focus on determining structural parameters in the excited states of medium-sized molecules (~30 atoms) in solution. The general methodology is set in a maximum-likelihood framework and is introduced through the analysis of the photoactive platinum compound PtPOP, in particular the structure of its lowest triplet excited state (3A2u). Emphasis is put on structure determination in terms of model comparisons and on the information content of difference scattering signals as well as the related experimental variables. Several suggestions for improving the accuracy of these types of measurements are presented.

Microtubule nucleation sequence studied by time-resolved x-ray scattering and electron microscopy

1983 ◽  
Vol 41 ◽  
pp. 766-767
Author(s):  
Eva-Maria Mandelkow ◽  
Eckhard Mandelkow ◽  
Joan Bordas
Keyword(s):  
Electron Microscopy ◽  
Dynamic Equilibrium ◽  
Time Resolved ◽  
X Ray ◽  
Additional Information ◽  
X Ray Scattering ◽  
Low Concentrations ◽  
Microtubule Growth ◽  
Ray Patterns ◽  
Ray Scattering

When a solution of microtubule protein is changed from non-polymerising to polymerising conditions (e.g. by temperature jump or mixing with GTP) there is a series of structural transitions preceding microtubule growth. These have been detected by time-resolved X-ray scattering using synchrotron radiation, and they may be classified into pre-nucleation and nucleation events. X-ray patterns are good indicators for the average behavior of the particles in solution, but they are difficult to interpret unless additional information on their structure is available. We therefore studied the assembly process by electron microscopy under conditions approaching those of the X-ray experiment. There are two difficulties in the EM approach: One is that the particles important for assembly are usually small and not very regular and therefore tend to be overlooked. Secondly EM specimens require low concentrations which favor disassembly of the particles one wants to observe since there is a dynamic equilibrium between polymers and subunits.

Time-Resolved Cryo-Electron Microscopy of Oscillating Microtubules

1990 ◽  
Vol 48 (1) ◽  
pp. 502-503
Author(s):  
Eva-Maria Mandelkow ◽  
Ron Milligan
Keyword(s):  
Electron Microscopy ◽  
Dynamic Instability ◽  
Entire Solution ◽  
Reaction Scheme ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
A Chain ◽  
Ray Scattering

Microtubules form part of the cytoskeleton of eukaryotic cells. They are hollow libers of about 25 nm diameter made up of 13 protofilaments, each of which consists of a chain of heterodimers of α-and β-tubulin. Microtubules can be assembled in vitro at 37°C in the presence of GTP which is hydrolyzed during the reaction, and they are disassembled at 4°C. In contrast to most other polymers microtubules show the behavior of “dynamic instability”, i.e. they can switch between phases of growth and phases of shrinkage, even at an overall steady state [1]. In certain conditions an entire solution can be synchronized, leading to autonomous oscillations in the degree of assembly which can be observed by X-ray scattering (Fig. 1), light scattering, or electron microscopy [2-5]. In addition such solutions are capable of generating spontaneous spatial patterns [6].In an earlier study we have analyzed the structure of microtubules and their cold-induced disassembly by cryo-EM [7]. One result was that disassembly takes place by loss of protofilament fragments (tubulin oligomers) which fray apart at the microtubule ends. We also looked at microtubule oscillations by time-resolved X-ray scattering and proposed a reaction scheme [4] which involves a cyclic interconversion of tubulin, microtubules, and oligomers (Fig. 2). The present study was undertaken to answer two questions: (a) What is the nature of the oscillations as seen by time-resolved cryo-EM? (b) Do microtubules disassemble by fraying protofilament fragments during oscillations at 37°C?

In situ Time-Resolved Small-Angle X-ray Scattering Reveals the Formation Kinetics of Polyelectrolyte Complex Micelles

2019 ◽  
Author(s):  
Hao Wu ◽  
Jeffrey Ting ◽  
Siqi Meng ◽  
Matthew Tirrell
Keyword(s):  
Small Angle ◽  
Self Assembly ◽  
Electrostatic Interactions ◽  
Polyelectrolyte Complex ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Kinetics Of ◽  
Ray Scattering

We have directly observed the <i>in situ</i> self-assembly kinetics of polyelectrolyte complex (PEC) micelles by synchrotron time-resolved small-angle X-ray scattering, equipped with a stopped-flow device that provides millisecond temporal resolution. This work has elucidated one general kinetic pathway for the process of PEC micelle formation, which provides useful physical insights for increasing our fundamental understanding of complexation and self-assembly dynamics driven by electrostatic interactions that occur on ultrafast timescales.

Time-Resolved, in Situ, Small- and Wide-Angle X-ray Scattering To Monitor Pt Nanoparticle Structure Evolution Stabilized by Adsorbed SnCl3– Ligands During Synthesis

2013 ◽  
Vol 117 (15) ◽  
pp. 7924-7933 ◽  
Author(s):  
Samuel St. John ◽  
Naiping Hu ◽  
Dale W. Schaefer ◽  
Anastasios P. Angelopoulos
Keyword(s):  
Structure Evolution ◽  
Wide Angle ◽  
Pt Nanoparticle ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Nanoparticle Structure ◽  
Ray Scattering

scholarly journals Arguments for an additional long-lived intermediate in the photocycle of the full-length aureochrome 1c receptor: A time-resolved small-angle X-ray scattering study

2019 ◽  
Vol 6 (3) ◽  
pp. 034701 ◽  
Author(s):  
Saskia Bannister ◽  
Elena Böhm ◽  
Thomas Zinn ◽  
Thomas Hellweg ◽  
Tilman Kottke
Keyword(s):  
Small Angle ◽  
Full Length ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Scattering Study ◽  
Ray Scattering

scholarly journals Osmotic shrinkage of sterically stabilized liposomes as revealed by time-resolved small-angle X-ray scattering

2014 ◽  
Vol 47 (1) ◽  
pp. 35-40 ◽  
Author(s):  
Zoltán Varga ◽  
András Wacha ◽  
Attila Bóta
Keyword(s):  
Form Factor ◽  
Small Angle ◽  
Freeze Fracture ◽  
Initial Step ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Sterically Stabilized Liposomes ◽  
Liposome Size ◽  
Ray Scattering

Time-resolved synchrotron small-angle X-ray scattering (SAXS) was used to study the structural changes during the osmotic shrinkage of a pharmacologically relevant liposomal drug delivery system. Sterically stabilized liposomes (SSLs) with a diameter of 100 nm and composed of hydrogenated soy phosphocholine, cholesterol and distearoyl-phosphoethanolamine-PEG 2000 prepared in a salt-free buffer were mixed with a buffered 0.3 MNaCl solution using a stopped flow apparatus. The changes in the liposome size and the bilayer structure were followed by using SAXS with a time resolution of 20 ms. A linear decrease in liposome size is observed during the first ∼4 s of the osmotic shrinkage, which reveals a water permeability value of 0.215 (15) µm s−1. The change in the size of the liposomes upon the osmotic shrinkage is also confirmed by dynamic light scattering. After this initial step, broad correlation peaks appear on the SAXS curves in theqrange of the bilayer form factor, which indicates the formation of bi- or oligolamellar structures. Freeze-fracture combined with transmission electron microscopy revealed that lens-shaped liposomes are formed during the shrinkage, which account for the appearance of the quasi-Bragg peaks superimposed on the bilayer form factor. On the basis of these observations, it is proposed that the osmotic shrinkage of SSLs is a two-step process: in the initial step, the liposome shrinks in size, while the area/lipid adapts to the decreased surface area, which is then followed by the deformation of the spherical liposomes into lens-shaped vesicles.

Time-resolved isothermal crystallization of absorbable PGA-co-PLA copolymer by synchrotron small-angle X-ray scattering and wide-angle X-ray diffraction

Polymer ◽  
2001 ◽  
Vol 42 (21) ◽  
pp. 8965-8973 ◽  
Author(s):  
Zhi-Gang Wang ◽  
Xuehui Wang ◽  
Benjamin S. Hsiao ◽  
Saša Andjelić ◽  
Dennis Jamiolkowski ◽  
...  
Keyword(s):  
Small Angle ◽  
Isothermal Crystallization ◽  
Wide Angle ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Simultaneous time-resolved synchrotron X-ray scattering studies on block copoly(ether-urethane) phase behaviour

1995 ◽  
Vol 97 (1-4) ◽  
pp. 253-256 ◽  
Author(s):  
S. Naylor ◽  
W. Bras ◽  
G. Derbyshire ◽  
G.R. Mant ◽  
D. Bogg ◽  
...  
Keyword(s):  
Phase Behaviour ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering
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