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Crystal Former Conference Presentations
MCSG PDB Deposits
The MCSG suite was adopted at the Midwest Center for Structural Genomics as the primary initial crystallization screen for PSI:Biology. The structures listed below have been determined directly from the respective crystallization condition provided without additional optimization. A far greater number of structures have been determined from the MCSG Suite following optimization of the initial conditions. These have not been provided here.
Overall Statistics To Date:
Total Number of Deposited Structures from ALL PSI:Biology Centers: 444
Structures from the MCSG Alone:
Total Number of Deposited Structures: 122
Structures obtained directly from MCSG Conditions: 67 (without optimization)
Structures obtained directly from MCSG1: 31
Structures obtained directly from MCSG2: 17
Structures obtained directly from MCSG3: 11
Structures obtained directly from MCSG4: 8
Last Updated: February 1, 2012
MCSG1 Successes
MCSG2 Successes
MCSG3 Successes
MCSG4 Successes
MCSG Crystallization Screen References
(1) Kim Y, Babnigg G, Jedrzejczak R, Eschenfeldt WH, Li H, Maltseva N, Hatzos-Skintges C, Gu M, Makowska-Grzyska M, Wu R, An H, Chhor G & Joachimiak A. (2011) High-throughput protein purification and quality assessment for crystallization. Methods 55(1): 12-28. DOI: 10.1016/i.ymeth.2011.07.010
Crystal Former - Customer Stories
(1) Crystallization and imaging of fluorescent protein crystals using the Crystal Former
Crystal Formers have been implemented in a number of product development ventures in recent months. In one such project, an RNA binding protein from the hyperthermophile Thermococcus thioreducens was crystallized using the high throughput Crystal Formers (CF-HT) by Dr. Marc Pusey of iXpressGenes. The protein was trace labeled with approximately 0.3% carboxyrhodamine. Images were produced as part of a project to develop a low-cost fluorescence and white light plate imager. This work also demonstrates the ability of this new device to image volumes as low as 30 nL.

(2) Bacterial Drug Targets
Methicillin-resistant Staphylococcus aureus and Helicobacter pylori are two major bacterial pathogens with direct impact on human health. MRSA exhibits resistance to the broad-spectrum antibiotics commonly used to treat staph strains. Most MRSA infections occur in hospitals and related health care centers and is responsible for serious skin and soft tissue infections and for a serious form of pneumonia. H pylori are resident in the stomachs and small intestines of approximately 50% people world-wide. While for many people H. pylori infection is asymptomatic, it is responsible for most ulcers, many cases of stomach inflammation and stomach cancer. Researchers at the University Health Network, led by Dr. Nickolay Chirgadze, have been investigating the protein structures of numerous proteins unique to these pathogenic bacteria with the intention of finding novel drug targets. Of three proteins that initially failed the vapor diffusion-based crystallization screening, two were successfully crystallized using only the standard 48 conditions that comprise the SmartScreen™ and the Crystal Former™. Furthermore, crystallization conditions for both proteins could be readily translated into vapor diffusion with minimal optimization.

(3) LeuT Integral Membrane Protein
Integral membrane proteins comprise a highly challenging class of structural biology targets. The LeuT transporter has a bundle of 12 alpha-helices that for a transport channel through the cell membrane and plays an important role in synapse clearage following the transduction of a nerve signal. Many antidepressant drugs, and recreational drugs, target LeuT and similar transporters, thus structural knowledge of the transport mechanism and recognition therapeutics is a high importance. Recent crystal trials with the Crystal Former have resulted in the identification of crystallization conditions for the LeuT transporter.
(4) Malaria Drug Targets
Malaria is a life-threatening disease caused by the
Plasmodium parasite that is transmitted to the human host through mosquito bites. In 2008, the World Health Organization recorded 247 million cases of malaria and almost 1 million deaths. In Africa, a child dies every 45 seconds from malarial infection, accounting for 20% of childhood deaths. Growing resistance to antimalarial treatment has spread rapidly in recent decades, undermining malaria control efforts. Structure-guided identification of novel therapeutic protein targets from
Plasmodium species and the further characterization of inhibitory complexes for such targets has become a key approach in the search for new malaria therapies. One such protein has been crystallized by
Dr. Terese Bergfors using the
Crystal Former.

(3) Stojanoff V, Jakoncic J, Oren DA, Nagarajan V, Navarro Poulsen JC, Adams-Cioaba MA, Bergfors T & Sommer MOA (2011). From Screen to structure with a harvestable microfluidic device. Acta Cryst F67:971-975. DOI:10.1107/S174430911102445
(2) Stewart PDS, Kolek SA, Briggs RA, Chayen NE & Baldock PFM (2011) Random microseeding: a theoretical and practical exploration of seed stability and seeding techniques for successful protein crystallization. Cryst. Growth Des. DOI: 10.1021/cg2001442.
(1) Terese Bergfors (2009) The rapid crystallization strategy for structure-based inhibitor design. From molecules to medicines: Structure of biological macromolecules and its relevance in combating new diseases and bioterrorism. Sussman JL & Spadon P. Eds. ISBN 978-90-481-2337-7
Crystal Former - Conference Presentations
(1) Weger A, Kim YC, Adams-Cioaba MA, Sommer M & Joachimiak A (2010) Microfluidic Crystal Formers for high throughput screening and optimization. NIGMS Workshop: Enabling technologies in structure and function. View Here