Proteins are individual things. It should be easy to test whether your
particular protein is stable and active with a given concentration of DMSO by
adding DMSO without the drug molecule. Add the DMSO, then check with light
scattering or SAXS for unfolding effects, or perhaps you have a spectroscopic
or activity assay you could run.
If your protein can tolerate DMSO, you get an added bonus in that DMSO is a
cryoprotectant.
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All Things Serve the Beam
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David J. Schuller
modern man in a post-modern world
MacCHESS, Cornell University
[email protected]
________________________________
From: CCP4 bulletin board <[email protected]> on behalf of amit gaur
<[email protected]>
Sent: Wednesday, October 2, 2024 2:51 PM
To: [email protected] <[email protected]>
Subject: [ccp4bb] Co-Crystallization with drug molecule
Hi everyone,
I am trying to crystallize a protein with a drug molecule. The protein
concentration is 15.5 mg/ml, the drug stock concentration is 10 mM, and the
drug is dissolved in DMSO. I am adding the drug to a final concentration of 1
mM in 100 ul of protein, and the DMSO volume is 10 ul for Co-crystallization. I
want to know how much DMSO is permissible during co-crystallization with the
drug and if DMSO can poison crystal formation. I have not been successful in
getting crystals with inhibitors till now, but I obtained crystals of protein
without DMSO, and those diffracted to 2.5A.
Thanks,
Dr. Amit Gaur,
Research Scientist
Center for Biotechnology and Interdisciplinary Studies,
Rensselaer Polytechnic Institute,
1623 15th Street, Troy, NY, 12180
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