Euler implicit time-discretization of multivariable sliding-mode controllers.

This paper aims to develop the Euler implicit time-discretization of multivariable sliding-mode controllers to solve the numerical chattering problem without modifying the continuous-time control law. To this end, a continuous-time multi-input plant under a multivariable sliding-mode control is studied, and it is shown that the implicit discretization of the continuous-time sliding-mode controller leads to a multivariable generalized equation with several set-valued terms which is not possible to be solved using the graphical interpretations. Subsequently, an algorithm is proposed to solve such a multivariable generalized equation required to synthesize the implicit sliding-mode control signal at each time step. The proposed algorithm is explained through a simple example accompanied by numerical simulations. The properties of the implicit multivariable sliding-mode controller, e.g., finite-time convergence, gain insensitivity, and chattering suppression, are studied analytically. Afterwards, a multivariable sliding-mode controller is implemented on a digital processor based on the developed algorithm to control a six-input six-output system, i.e., six-component thrust generator, and the results are compared with the case where the continuous-time sliding-mode controller is implemented using the conventional Euler explicit discretization. In the end, the related issues and drawbacks are addressed to be considered in future works.

Microfluidic chips for the crystallization of biomacromolecules by counter-diffusion and on-chip crystal X-ray analysis.

Microfluidic devices were designed to perform on micromoles of biological macromolecules and viruses the search and the optimization of crystallization conditions by counter-diffusion, as well as the on-chip analysis of crystals by X-ray diffraction. Chips composed of microchannels were fabricated in poly-dimethylsiloxane (PDMS), poly-methyl-methacrylate (PMMA) and cyclo-olefin-copolymer (COC) by three distinct methods, namely replica casting, laser ablation and hot embossing. The geometry of the channels was chosen to ensure that crystallization occurs in a convection-free environment. The transparency of the materials is compatible with crystal growth monitoring by optical microscopy. The quality of the protein 3D structures derived from on-chip crystal analysis by X-ray diffraction using a synchrotron radiation was used to identify the most appropriate polymers. Altogether the results demonstrate that for a novel biomolecule, all steps from the initial search of crystallization conditions to X-ray diffraction data collection for 3D structure determination can be performed in a single chip.

Structure of liquid films of an ordered foam confined in a narrow channel.

A bamboo foam is the simplest case of an ordered foam confined in a narrow channel. It is made of a regular film distribution, arranged perpendicularly to the channel. Our work consists of studying the structural properties of several films taken in a drained foam. X-ray experiments highlighted the equality of the equilibrium thickness for each film within a foam. The same thickness was found as by measurements of disjoining pressure isotherms, proving as well that films of a bamboo foam behave like isolated ones. The refinement of X-ray data by a simple model of specular reflectivity showed a significant variation of the electronic distribution of the surfactant layer for a common black film forwarding from one equilibrium state to another. A discussion on the organization of the surfactant molecules to the gas/liquid interface and film is proposed.

Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.

Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (SOR), a nonheme mononuclear iron enzyme that scavenges superoxide radicals. X-ray diffraction data at 1.95 angstrom resolution and Raman spectra recorded in crystallo revealed iron-(hydro)peroxo intermediates with the (hydro)peroxo group bound end-on. The dynamic SOR active site promotes the formation of transient hydrogen bond networks, which presumably assist the cleavage of the iron-oxygen bond in order to release the reaction product, hydrogen peroxide.

UV laser-excited fluorescence as a tool for the visualization of protein crystals mounted in loops.

Structural proteomics has promoted the rapid development of automated protein structure determination using X-ray crystallography. Robotics are now routinely used along the pipeline from genes to protein structures. However, a bottleneck still remains. At synchrotron beamlines, the success rate of automated sample alignment along the X-ray beam is limited by difficulties in visualization of protein crystals, especially when they are small and embedded in mother liquor. Despite considerable improvement in optical microscopes, the use of visible light transmitted or reflected by the sample may result in poor or misleading contrast. Here, the endogenous fluorescence from aromatic amino acids has been used to identify even tiny or weakly fluorescent crystals with a high success rate. The use of a compact laser at 266 nm in combination with non-fluorescent sample holders provides an efficient solution to collect high-contrast fluorescence images in a few milliseconds and using standard camera optics. The best image quality was obtained with direct illumination through a viewing system coaxial with the UV beam. Crystallographic data suggest that the employed UV exposures do not generate detectable structural damage.

Automated analysis of vapor diffusion crystallization drops with an X-ray beam.

Crystallogenesis, usually based on the vapor diffusion method, is currently considered one of the most difficult steps in macromolecular X-ray crystallography. Due to the increasing number of crystallization assays performed by protein crystallographers, several automated analysis methods are under development. Most of these methods are based on microscope images and shape recognition. We propose an alternative method of identifying protein crystals: by directly exposing the crystallization drops to an X-ray beam. The resulting diffraction provides far more information than classical microscope images. Not only is the presence of diffracting crystals revealed, but also a first estimation of the space group, cell parameters, and mosaicity is obtained. In certain cases, it is also possible to collect enough data to verify the presence of a specific substrate or a heavy atom. All these steps are performed without the sometimes tedious necessity of removing crystals from their crystallization drop.

A new highly integrated sample environment for protein crystallography.

Protein crystallography is becoming a popular technique that is routinely used to access structural information. At one end of the process, sample preparation is now facilitated by commercially available crystallization kits. At the other end, structure determination has been made easier by automated software. Data collection, the step in between, is now usually performed on synchrotron sources. However, it is still restricted to experienced users and requires significant help from beamline staff. Part of this difficulty arises from the sophisticated experimental setup, which comprises a goniometer, a magnetic head, a device for changing the sample and monitoring accessories. It was proposed that this setup could be simplified by replacing these elements by a robotic arm that can perform all of the required tasks. In the present paper, it is demonstrated that this new setup can be used on a synchrotron beamline to mount and centre the sample and to collect diffraction data. This new system completely changes the design of the experimental setup by merging functions that were previously considered to be distinct. Moreover, automation of sample handling need not be considered as a specific development and is now included in a unique multipurpose device.