|New Developments for a Full Automation of the FIP Beamline at the ESRF|
Jacquamet L., Bertoni A., Borel F., Charrault P., Israel-Gouy P., Iwema T., Kahn R., Joly J., Ohana J., Pirocchi M., Robin A., Serre L., Vernede X. and Ferrer J. L.
FIP (French beamline for the Investigation of Proteins) at the ESRF (European Synchrotron Radiation Facility) pushed developments in automation to reach a fully automated beamline. - The energy adjustment and beam optimization are completely automated. - The screening of the different protein crystals is ensured by a robotic system.In addition, this robot offers the possibility to analyze crystals directly as they grow in drops inside crystallization plates.
|Insights into the Mechanism of Partial Agonism: Crystal Structures of the Peroxisome Proliferator-activated Receptor-gamma Ligand-Binding Domain in the Complex with Two Enantiomeric Ligands|
Giorgio Pochetti, Cristina Godio, Nico Mitro, Donatella Caruso, Samuele Scurati, Andrea Galmozzi, Fulvio Loiodice, Giuseppe Fracchiolla, Paolo Tortorella, Antonio Laghezza, Antonio Lavecchia, Ettore Novellino, Fernando Mazza, Maurizio Crestani
The peroxisome proliferator-activated receptors (PPARs) are transcriptional regulators of glucose and lipid metabolism. They are activated by natural ligands, such as fatty acids, and are also target of synthetic antidiabetic and hypolipidemic drugs. By using cell-based reporter assays, we studied the transactivation activity of two enantiomeric ureidofibrate derivatives.
|Methods For Automated Structure Determination for Ligands Within a Protein-Ligand Complex|
Gregory L. Warren and Matthew T. Stahl
Afitt is a software package for automated ligand conformation generation and placement within algorithmically identified unfilled electron density. Following real space refinement, the ligand solution is sent for subsequent refinement by Refmac or CNX, via coordinate and dictionary files. We have validated Afitt on forty publicly available data sets, chosen because it contains examples of highly strained ligand conformations.
|Automated, Low Volume Dynamic Light Scattering Technology to Accelerate Protein Crystallization|
Kevin Jackson and Robert Collins
The quest for solving protein structure largely relies upon X-Ray diffraction, a method requiring crystalline forms of the target protein. Among the many steps comprising structure determination, the process of protein crystallization represents one of the most significant, time-consuming challenges. A new low sample volume, automated dynamic light scattering (DLS) technology has been developed – the DynaPro Plate Reader.
|A Solution for Low Volume Pipetting Applications Requiring High Accuracy of Sample Placement|
Joby Jenkins, Rob Lewis, Tristan Cope and Chloë Milburn
Mosquito’s unique positive displacement disposable tips and precise X, Y and Z movements allow smaller drops with accurate and repeatable volumes to be positioned very precisely. This ability is essential for successful assay miniaturisation and the set-up of more effective serial dilutions or protein crystallography screens.
|Facilitating Low Volume Protein Crystallography Set-ups Using the Mosquito® Liquid Handler|
Jas Sanghera, Joby Jenkins, Rob Lewis, Chloe Milburn
The mosquito® (TTP LabTech) offers fast positive displacement pipettingfor accurate and reproducible aspiration and dispensing throughout the 50 nL-1.2 µL range, producing CVs of <8% at 50 nLirrespective of viscosity. Mosquito’s micropipettes are also disposable, thus guaranteeing zero cross-contamination where required.
|From Medicinal Plants to Bioactive Drugs|
Ilaria Lampronti, Mahmud T.H. Khan, Antoine M. Saab, Elisabetta Lambert, Letizia Penolazzi, Roberta Piva and Roberto Gambari
The aim of our study was to analyze the antiproliferative activity effects on human tumor cell lines and the differentiating activity on human erythroleukemic K562 cells of different extracts derived from medicinal plants of Bangladesh and Lebanon.
|Rapid and Miniaturized Robotic Crystallization Experiment using the Honeybee 963™ System|
Malcolm Willson, Hamid Khoja and Charles Dang
The Honeybee 963 for automated sitting drop crystallization studies enables rapid, precise and accurate dispensing of nano-liter (nl) volumes of screening and protein solutions. Rapid dispensing to both reservoirs and shelves minimizes evaporation while precise and accurate dispensing allows for miniaturization and conserves precious protein.
|High-Quality Protein Crystallization in Space|
Ari Yamanaka, et. al.
JAXA (Japan Aerospace Exploration Agency) has developed and established ultra-high quality protein crystallization technology using microgravity environments. High-quality protein crystals were grown based on technical improvements. Growing high-quality protein crystals in space can help better understand 3-dimensional protein structure.
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