BACKGROUND: Recently we acquired an Art Robbins Phoenix
crystallization robot. This instrument is in a shared environment,
accessible to labs with projects that range from small, well-behaved
soluble cytosolic proteins to large complexes and integral membrane
proteins. Many of our users obtain only small quantities (a few
hundred microliters) of purified proteins, and they are always
looking for ways to maximize the number of crystallization screens
they can set up with their samples.
QUESTION: Several users have recently asked if they could use a
protocol that allows them to aspirate enough protein into the
Nanoneedle (the needle used for dispensing protein) to set up 3-5 or
more different 96-condition screens. They feel this would minimize
any sample waste and maximize their time. Our concern is that this
might result in clogging of the Nanoneedle due to evaporation and
subsequent precipitation of their protein, as the amount of time
required for such a protocol would be greater than 10 minutes. Our
local Art Robbins representative has agreed with us that this is not
a recommended protocol. We are in a bit of a dilemma as we do not
have enough experience with this robot to definitively say that the
users should not follow this kind of protocol, but perhaps there is a
better way to achieve their desired goal.
Does anyone out there have any practical suggestions and experience
that could help us accommodate such user requests?
Thank you in advance, I'll post a summary of responses,
Diana
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Diana R. Tomchick
Associate Professor
University of Texas Southwestern Medical Center
Department of Biochemistry
5323 Harry Hines Blvd.
Rm. ND10.214B
Dallas, TX 75390-8816, U.S.A.
Email: [EMAIL PROTECTED]
214-645-6383 (phone)
214-645-6353 (fax)
