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THURSDAY, JANUARY 12
7:30 am Breakfast Presentation (Sponsorship Opportunity Available) or Morning Coffee
8:15 Chairperson’s Remarks
Ray Owens, Ph.D., NDM Senior Research Fellow, Division of Structural Biology, Oxford Protein Production Facility, University of Oxford
8:20 Identification of Chromatographic Steps for Protein Purification using Parallel Screening Methods
Kaushal Rege, Ph.D., Assistant Professor, Chemical Engineering, Ira A. Fulton School of Engineering, Arizona State University - Biography
This presentation will describe the use of miniaturized parallel screening approaches for the rapid identification of chromatographic steps required for purification of target proteins from culture broths. Microtiter well plate based screens were employed for identifying appropriate modes and operating conditions for a single chromatographic step. Enriched bioproduct from a chromatographic step was then used as feed in order to identify subsequent chromatographic steps in the screen. This screening method can be repeated across multiple chromatographic dimensions, leading to the identification of chromatographic steps that can result in high purities of the target protein.
8:50 Expressing the Human Proteome: Optimizing Expression and Purification for High-Throughput Protein Production
Opher Gileadi, Ph.D., Principal Investigator, Biotechnology and Genomic Integrity, The Structural Genomics Consortium (SGC), University of Oxford - Biography
The Stuctural Genomics Consortium has faced the challenge of producing thousands of unique human proteins in amounts and purity suitable for crystallization, screening assays, and antibody generation. The talk will describe the methods of production and purification in E. coli and Baculovirus, which provide a guidance for developing purification schemes for new proteins.
9:20 Large-Scale, High-Throughput Gene Cloning, Expression and Purification of Recombinant Proteins
Andrzej Joachimiak, Ph.D., Argonne Distinguished Fellow, Director, Structural Biology Center & Midwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory
9:50 Sponsored Presentation (Opportunity Available)
10:05 Networking Coffee Break in the Exhibit Hall, Poster Awards
10:45 Identification of Protein Refolding Conditions
Bruno Antonsson, Ph.D., Senior Scientist & Head, Protein Biochemistry, Merck Serono SA Geneva
Recombinant proteins are frequently recovered as inclusion bodies when expressed in bacteria. The proteins then need to be denatured and refolded into their native active structure. The refolding process often can be the limiting step for purification and production of recombinant proteins expressed in bacteria. Using a two-step 96-well based and design of experiments supported refolding screen, optimized refolding conditions can be identified with 50 mg of solubilized inclusion bodies in less than 2 weeks. For proteins where refolding conditions were already available, the new refolding conditions identified increased the yields up to 10 fold.
11:15 IT Partnership to Enable High-Throughput Process Development
Paul Hanson, Ph.D., Staff Engineer II, Cambridge Biologics CMC Group, Millennium Pharmaceuticals - Biography
Data management is becoming increasingly important in order to deliver just-in-time information that can be used for decision making, such as information from process development in control strategies to determine the impact of an OOS/OOT. This talk will address how to process and track 3000 samples per week while maintaining traceability, and will touch on the current state of data management and pain points. Also, I will discuss an IT roadmap for integrating lab data systems with SDMS and ELNs.
11:45 What Can a LIMS Do for Protein Scientists?
Chris Morris, Computational Science and Engineering Department, Science and Technology Facilities Council (STFC) - Biography
Protein Information Management System (PiMS) is a laboratory information management system (LIMS) for protein production. PiMS supports the archiving and sharing of research data. The basic concepts of PiMS are targets, constructs, samples, and experiments. Protocols can be recorded in PiMS and serve as a template for individual experiments. PiMS is designed to support both high-throughput methods and hypothesis driven work. It is especially suitable for long term projects, scattered collaborations, and service provision. The presentation will discuss the benefits and disadvantages of using a LIMS for protein production in general, and protein purification in particular.
12:15 pm Close of Morning Session
12:30 Luncheon Presentations (Sponsorship Opportunity Available) or Lunch on Your Own
1:30 End of Conference
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Links to Companion Meetings
Protein Aggregation and Emerging Analytical Tools
Protein Purification & Recovery