|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.
|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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