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Saturday, October 25, 2014
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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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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High-Throughput and High-Yield Purification of Recombinant Proteins Expressed in Escherichia coli.
Chiann-Tso Lin, Priscilla A. Moore, Deanna L. Auberry, Kristin D. Victry, Frank R. Collart and Vladimir Kery

We have developed a high throughput expression of recombinant proteins containing hexahistidine affinity tag in Escherichia coli followed by one step affinity purification of proteins on Ni2+ agarose beads.

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Showing Results 21 - 29 of 29
Scientific News
Major Step Forward in Understanding of Viruses
Scientists unlock exact structure of Hepatitis A virus.
Crystallizing the DNA Nanotechnology Dream
Scientists have designed the first large DNA crystals with precisely prescribed depths and complex 3D features, which could create revolutionary nanodevices.
Breakthrough Allows Researchers to Watch Molecules “Wiggle”
A new crystallographic technique developed at the University of Leeds is set to transform scientists’ ability to observe how molecules work.
X-Ray Free Electron Laser for Fixed-Target Protein Serial Microcrystallography
The article presents the first proof-of-principle results from fixed-target serial crystallography using the Linac Coherent Light Source.
Identifying, Studying and Making Good Use of Macromolecular Crystals
Techniques that extend the observation of crystals beyond the optical microscope will enhance structural biology in the future.
'Evolved' Protein May Stop Cancer From Spreading
Experimental therapy stopped the metastasis of breast and ovarian cancers in lab mice, pointing toward a safe and effective alternative to chemotherapy.
Protein Crystalline Frameworks: A New Class of Materials
Scientists at the Helmholtz Center Berlin (HZB) along with researchers at China’s Fudan University have characterized a new class of materials called protein crystalline frameworks (PCFs).
Worm Virus Details Come to Light
Rice University scientists have won a race to find the crystal structure of rare nematode virus, known to infect the most abundant animal on Earth.
Structure of Molecular Machine for Targeted Viral DNA Destruction Determined
The MSU-led research provides the first detailed blueprint of a multi-subunit “molecular machinery” that bacteria use to detect and destroy invading viruses.
Flu’s Mechanisms Clues Uncovered
Researchers from Rice University and Baylor College of Medicine have analyzed how influenza-related proteins help infect cells.
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