One
of the primary bottlenecks in high throughput structural biology
is the identification of a suitable protein crystal and its subsequent
removal from the growth medium and mounting for crystallographic
investigation. Using a simple micromachined silicon holder (Si
Screens), the growth, harvesting, mounting and crystal quality
determination operations are performed as one seamless procedure
thereby abrogating many of the laborious and expensive operations
associated with protein crystallization.
The
advantages over the conventional methods are:
a) after the crystal growth , the crystal is harvested
without damage by simply removing the grid (~1 x 1 sqmm) along
with the crystal,
b) mother liquor is easily wicked away,
c) the grid/crystal can be placed directly into the x-ray
beam; single crystal Si has little low angle diffuse scatter and
the high lattice symmetry and excellent crystallinity produces
relatively few Bragg peaks and only at high 2q values,
d) by using an array of Si grids, the presence and quality
of protein crystals in an entire screening plate is automatically
determined by simply moving each library address into the x-ray
beam.
The
silicon screens will facilitate rapid screening of crystallization
results using X-ray diffraction and would dramatically revolutionize
the way high-throughput crystallography is conducted to date.
The tools and procedures currently under development are intended
to eliminate the final manual step in the workflow of automated
crystallography and will lead to a higher success rate in determining
crystallization conditions of new proteins.
Please contact
us for pricing and custom designing of the mounting
wands
