The manipulators used to support and position lattice elements are critical components of all particle accelerators. The increased use of large superconducting magnets and accelerator modules places even greater demands on these manipulators. However, the performance of these support systems has not kept pace with the advances made in other areas of accelerator technology. This results in accelerators that are difficult to align and may not be capable of achieving target luminosities. An innovative new type of positioning mechanism tailored to the requirements of the International Linear Collider is proposed. The Tri-Sphere System provides secure support for large lattice elements and precision adjustment in six degrees of freedom. Integrated target sockets allow the support system to be rapidly pre-aligned. The system's kinematic design passively guides lattice elements into their correct location during installation. A complimentary Portable Actuation Unit provides the advantages of automated adjustment and allows these adjustments to be completely decoupled from surveying.
The demonstration unit of the Universal Micromanipulation Robot (UMR) capable of semi-autonomous protein crystal harvesting has been tested and evaluated by independent users. We report the status and capabilities of the present unit scheduled for deployment in a high-throughput protein crystallization center. We discuss operational aspects as well as novel features such as micro-crystal handling and drip-cryoprotection, and we extrapolate towards the design of a fully autonomous, integrated system capable of reliable crystal harvesting. The positive to enthusiastic feedback from the participants in an evaluation workshop indicates that genuine demand exists and the effort and resources to develop autonomous protein crystal harvesting robotics are justified.
A precise, versatile, and automated method of orienting a sub-millimeter crystal in a focused neutron beam is required for efficient operation of the TOPAZ Single Crystal Diffractometer at the Spallation Neutron Source at Oak Ridge National Laboratory. To fulfill this need, a Compact Crystal Positioning System (CCPS) has been developed in collaboration with Square One Systems Design in Jackson, Wyoming. The system incorporates a tripod design with six vacuum-compatible piezoelectric linear motors capable of < 1μm resolution. National Instruments LabVIEW provides a means of system automation while at the same time accommodating the modular nature of the SNS sample environment control software for straightforward system integration. Results from an ambient test at the Advanced Photon Source at Argonne National Laboratory will be presented.
Poster Sessions lattices and establishes that indeed fluorine has a directing influence in molecular assembly.In order to evaluate the propensity of interactions in halogens in general ortho chloro and ortho bromo anilines were crystallized from their respective liquids via in situ cryocrystallization method.The crystal structures are isostructural belonging to a trigonal system, space group P 31.The crystal packing is due to intramolecular N-H...Cl or Br and intermolecular N-H...N hydrogen bonds.However, in the case of ortho bromo aninline short Br...Br contacts ( 3.64 Å) are observed suggesting that this interaction is a consequence of the size of Br atom. 1. Deepak Chopra and T. N.
One of the critical steps in high throughput crystallography that so far has evaded automation is the actual harvesting of the delicate crystals from the mother liquor in which they are growing. The late-stage operation of harvesting is presently a most risky and loss-intensive procedure, compounded by its tight integration with the critical steps of cryo-protection and cryo-quenching. Recent advances in micromanipulation robotics and micro-fabrication have made it possible to seriously consider automation of protein crystal harvesting. Based on the experience gained during the development of an operator-assisted (and now operator-assisting) universal micromanipulation robot (UMR) prototype, we discuss the challenges ahead for the design of a fully autonomous, integrated system capable of the reliable harvesting of protein microcrystals. Experience from participation in NIH structural genomics projects and feedback from bottleneck workshops indicates that genuine demand exists in the high throughput community as well as in pharmaceutical production pipelines, justifying the effort and resources to develop autonomous harvesting robotics.
High-throughput crystallography has reached a level of automation where complete computer-assisted robotic crystallization pipelines are capable of cocktail preparation, crystallization plate setup, and inspection and interpretation of results. While mounting of crystal pins, data collection and structure solution are highly automated, crystal harvesting and cryocooling remain formidable challenges towards full automation. To address the final frontier in achieving fully automated high-throughput crystallography, the prototype of an anthropomorphic six-axis universal micromanipulation robot (UMR) has been designed and tested; this UMR is capable of operator-assisted harvesting and cryoquenching of protein crystals as small as 10 µm from a variety of 96-well plates. The UMR is equipped with a versatile tool exchanger providing full operational flexibility. Trypsin crystals harvested and cryoquenched using the UMR have yielded a 1.5 Å structure demonstrating the feasibility of robotic protein crystal harvesting.
High-throughput crystallography has reached a level of automation where complete computer-assisted robotic crystallization pipelines are capable of cocktail preparation, crystallization plate setup, and inspection and interpretation of results. While mounting of crystal pins, data collection and structure solution are highly automated, crystal harvesting and cryocooling remain formidable challenges towards full automation. To address the final frontier in achieving fully automated high-throughput crystallography, the prototype of an anthropomorphic six-axis universal micromanipulation robot (UMR) has been designed and tested; this UMR is capable of operator-assisted harvesting and cryoquenching of protein crystals as small as 10 mm from a variety of 96-well plates. The UMR is equipped with a versatile tool exchanger providing full operational flexibility. Trypsin crystals harvested and cryoquenched using the UMR have yielded a 1.5 A ˚ structure demonstrating the feasibility of robotic protein crystal harvesting.