Scripps Research Institute Scientists Find Structure of Critical Ebola Virus Protein

Fluidigm's TOPAZ(R) Protein Crystallization System Helps Make this
Discovery
SOUTH SAN FRANCISCO, Calif.--(Business Wire)--
Scientists at the Scripps Research Institute have uncovered the
structure of a critical protein from the Ebola Virus that allows viral
entry in human cells.

"This structure reveals how this critical piece of the virus is
assembled and helps explain how the pathogen evades and exploits the
human immune system," explained Erica Ollmann Saphire, the Scripps
Research scientist who led the five-year effort.

There is currently no cure for Ebola hemorrhagic fever. The virus
is spread when people come into contact with the bodily fluids of
someone who is already infected. Most ultimately die from a
combination of dehydration, massive bleeding, and shock.

Described in the cover article of the July 10, 2008 issue of the
Nature magazine, the research reveals the shape of the Ebola virus
"spike" protein, which is necessary for viral entry into human cells.
The Scripps discovery of this structure provides a major step forward
in understanding how the deadly virus works, and may be useful in the
development of potential Ebola virus vaccines, or treatments for those
infected.

The Role of Fluidigm's TOPAZ(R) Protein Crystallization System

Scripps researchers generated more than one hundred versions of
the protein for crystallization studies. TOPAZ screening chips were
used to identify crystallization conditions, and vapor diffusion
methods were used to reproduce crystals suitable for X-ray
diffraction. The crystals were further optimized and X-ray diffraction
data was ultimately collected to 3.4 Angstroms.

"It is difficult to produce a lot of this protein, but the
possibility of screening on a small scale helped us find a GP-antibody
complex that would crystallize reproducibly," said Dr. Ollmann
Saphire.

TOPAZ screening chips are capable of running up to 768 experiments
in parallel using only 1 microliter of protein per 96 conditions. The
TOPAZ system also includes an effective analysis software for scoring
crystals and managing the vast amount of data obtained from
crystallization experiments.

A press release from the Scripps Research Institute describing
their discovery in greater technical detail is available at:
http://www.scripps.edu/newsandviews/e_20080714/ebola.html

In addition to Ollmann Saphire, the article, "Structure of the
trimeric, prefusion Ebola virus glycoprotein in complex with a
neutralizing antibody from a human survivor," include Jeffrey E. Lee,
Marnie L. Fusco, Ann J. Hessell, Wendelien B. Oswald, and Dennis R.
Burton at The Scripps Research Institute. For more information on the
paper, see the journal Nature for the paper's abstract (with links to
the full text) at
http://www.nature.com/nature/journal/v454/n7201/abs/nature07082.html

About Fluidigm

Fluidigm develops, manufactures and markets proprietary Integrated
Fluidic Circuit (IFC) systems that significantly improve productivity
in life science research. Fluidigm's IFCs enable the simultaneous
performance of thousands of sophisticated biochemical measurements in
extremely minute volumes. These "integrated circuits for biology" are
made possible by miniaturizing and integrating liquid handling
components on a single microfabricated device. Fluidigm's IFC systems,
consisting of instrumentation, software and single-use IFCs, increase
throughput, decrease costs and enhance sensitivity compared to
conventional laboratory systems. Fluidigm products have not been
cleared or approved by the Food and Drug Administration for use as a
diagnostic and are only available for research use.

For more information, please visit www.Fluidigm.com.

Fluidigm, the Fluidigm logo, Topaz, BioMark, and NanoFlex are
trademarks of Fluidigm Corporation.

Fluidigm Corporation
Howard High, 510-786-7378
Howard.high@fluidigm.com

Copyright Business Wire 2008