|
|
|
Provisional Agenda
(This agenda is subject to addition and change)
Day 1 - 19th June 2008
|
08:00 |
Registration |
|
08:55 |
Protein Chemistry and Crystallization
Session Chair: Naomi Chayen, Professor, Imperial College London |
|
09:00 |
The 3.4 A Resolution X-ray Crystal Structure of a Plant Photosystem I Supercomplex
Alexey Amunts, PhD Student, Tel Aviv University
Photosystem-I is multi-subunit membrane supercomplex of protein and non-protein components that drives the photosynthesis process. The intact structure is described at 3.4Å resolution. The structural information provides a first glimpse at the fine architecture of Nature’s most efficient photochemical machine. |
|
09:30 |
“Plain truth” of Crystallomic vs. “Heresy” of High Throughput Crystallization
Jan Sedzik, Associate Professor, Karolinska Institute
Comparison between technology of crystallomic, and high throughput crystallization. |
|
10:00 |
Coffee & Networking in the Exhibition Hall |
|
10:55 |
New Laboratory Instrumentation and Techniques |
|
11:00 |
New Insights into Biomolecule Crystallization Processes using Dynamic Light Scattering and Imaging in Multi-well Plates
Christian Betzel, Professor, University of Hamburg |
|
11:30 |
Towards the Design of a 'Universal' Nucleant for Protein Crystallization
Naomi Chayen, Professor, Imperial College London |
|
12:00 |
Title to be Confirmed |
|
12:30 |
Lunch & Poster Viewing |
|
14:25 |
Advances in Diffraction Techniques and Crystallographic Computing |
|
14:30 |
Fully Remote Access to SSRL Protein Crystallography Beam Lines
Clyde Smith, Staff Scientist, Stanford University
During the last user run (2007/2008), over 75% of the user groups have used the remote access tools available on the six protein crystallography beam lines at SSRL. This live remote access demonstration will showcase the features currently available to remote users. |
|
15:00 |
Automation, Robotics and Remote Access at the SSRL Protein Crystallography Beam Lines
Aina Cohen, Staff Scientist, Stanford University
The crystal screening and data collection component of the macromolecular crystallography experiment lends itself perfectly to automation. The design and implementation of the automated technologies enabling fully remote access to the SSRL macromolecular crystallography will be described. |
|
15:30 |
Coffee & Networking in Main Exhibition Hall |
|
16:30 |
Database for Structural data Using Semantic Web concepts to Support Structure-Based Drug Design for AIDS
T.N. Bhat, Project Leader, National Institute of Standards and Technology |
|
17:00 |
Drinks Reception in Main Exhibition Hall - Sponsorship available, contact paul.raggett@selectbiosciences.com |
Day 2 - 20th June 2008
|
08:55 |
Advances in Diffraction Techniques and Crystallographic Computing
Session Chair: Sir Tom Blundell, Professor of Biochemistry and Chair, School of Biological Sciences, University of Cambridge |
|
09:00 |
High-Throughput Protein Structure Determination Using Computational Grids
Ashley Buckle, Group Leader, Monash University
We have developed a simple web-based approach to testing tens to hundreds of molecular replacement (MR) search models using a modest lab-based grid. The second approach entails exhaustive MR using the entire PDB. All software is open source.
|
|
09:30 |
The PX Scanner: In-situ X-Ray Inspection of Protein Crystals in multi-Well Plates
Marcus Winter, Manager, Oxford Difraction |
|
10:00 |
Coffee & Networking in Main Exhiition Hall |
|
11:00 |
High-Throughput Protein Crystallography and Drug Discovery
Sir Tom Blundell, Professor of Biochemistry and Chair, School of Biological Sciences, University of Cambridge
The knowledge of the three-dimensional structures of protein targets that is now emerging from structural proteomics and targeted structural biology programmes has the potential to increase our understanding of human genetic variation, as well as to accelerate drug discovery. |
|
11:30 |
Crystal Structure of CapB, a Tyrosine Kinase from the Pathogen Staphylococcus Sureus
Slyvie Nessler, Professor, CNRS
This work presents the structural analysis of a bacterial tyrosine kinase implicated in the pathogenicity of the human pathogen Staphylococcus aureus. It allowed us to explain the catalytic and regulation mechanisms of this interesting drug design target. |
|
12:00 |
Lunch & Poster Presentations |
|
14:00 |
Probing the Substrate Specificity and Mechanism of EstB Esterase from Lactobacillus Rhamnosus
Gillian Norris, Senior Lecturer, Massey University
Structures of EstB, an esterase from the dairy lactic acid bacterium Lactobacillus rhamnosus have been solved in the presence of a number of substrate analogue inhibitors. Comparisons of the rates of inhibition and enzyme-inhibitor structures have provided an insight into the substrate specificities and mechanism of EstB. |
|
14:30 |
A Rapid Method for Determining Shape and Cross Sections of Macromolecular Complexes
Iain Campuzano, Waters Corp |
|
15:00 |
Coffee & Networking |
|
16:00 |
Title to be Confirmed |
|
16:30 |
Close of Conference |
|