A worldwide e-Infrastructure for NMR and structural biology

Tomas Malinauskas (Cold Spring Harbor Laboratory)

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Cold Spring Harbor Laboratory
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Cold Spring Harbor Laboratory is a world-renowned, private research and education institution with research programs in Cancer, Neuroscience, Plant Biology, Quantitative Biology, and Bioinformatics & Genomics. The research environment is highly collaborative, allowing CSHL scientists to work together across disciplines to solve biology’s most challenging problems. The ultimate goal is to apply this research on basic biological mechanisms to improve the diagnosis and treatment of cancer, neurological disorders and other diseases.

Research at the Laboratory is enriched by collaborations with scientists at other universities, hospitals, and in the biotech and pharmaceutical sectors. Scientific interaction and exchange of new ideas within the institution's research community is enhanced by a robust Meeting and Courses program that attracts approximately 9,850 scientists from around the world each year to CSHL facilities on Long Island.  A new meeting venue in China attracts an additional 2,650 participants.

The innovative spirit, vision, and talent of the Laboratory’s scientists continue to place CSHL among the top 1% of life science institutions most cited in published research. The dynamic, collaborative environment at CSHL also fosters a superb educational experience for an outstanding group graduate students and postdoctoral researchers.

Structural Biology
Postdoctoral research scientist
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I am a postdoctoral research scientist from Dr. Hiro Furukawa's group at the Cold Spring Harbor Laboratory, New York. I use a range of biochemical (insect and mammalian cell-based protein expression and purification, cell-based assays), biophysical (X-ray crystallography, surface plasmon resonance and multi-angle light scattering) and bioinformatics methods to elucidate the molecular mechanisms of cell-to-cell communication. I aim to understand the way these mechanisms are integrated to create and maintain living organisms.

In addition, I provide a structural perspective on protein structure-function relationships on a collaborative basis, e.g. analyses of mutations from the next generation sequencing data, mapping these mutations onto protein 3D structures, assessing potential implications on protein function, and presenting results in the publication-ready figures. Please feel free to contact me if you have any questions.

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Structural biology; X-ray crystallography; protein structure; determination, refinement and analysis of macromolecular crystal structures; protein structure-function relationships; molecular graphics; homology modelling; evolutionary analysis; PyMOL
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Cite WeNMR/WestLife

Usage of the WeNMR/WestLife portals should be acknowledged in any publication:
"The FP7 WeNMR (project# 261572) and H2020 West-Life (project# 675858) European e-Infrastructure projects are acknowledged for the use of their web portals, which make use of the EGI infrastructure and DIRAC4EGI service with the dedicated support of CESNET-MetaCloud, INFN-PADOVA, NCG-INGRID-PT, RAL-LCG2, TW-NCHC, SURFsara and NIKHEF, and the additional support of the national GRID Initiatives of Belgium, France, Italy, Germany, the Netherlands, Poland, Portugal, Spain, UK, South Africa, Malaysia, Taiwan and the US Open Science Grid."
And the following article describing the WeNMR portals should be cited:
Wassenaar et al. (2012). WeNMR: Structural Biology on the Grid.J. Grid. Comp., 10:743-767.


The WeNMR Virtual Research Community has been the first to be officially recognized by the EGI.

European Union

WeNMR is an e-Infrastructure project funded under the 7th framework of the EU. Contract no. 261572

WestLife, the follow up project of WeNMR is a Virtual Research Environment e-Infrastructure project funded under Horizon 2020. Contract no. 675858