clarsen at bimcore.emory.edu
Fri Sep 23 07:48:39 EST 1994
I have a protein that my collaborator has been trying to crystallize for
three years now. We have a native data set to 3.8 A. Unfortunately,
the heavy atom derivative has been unstable.
My strain is the BL21 variety, and uses a T7 promoter. I think that the
met auxotroph of this strain is available, so that a seleno met version
could easily be created. I can purify 100 mg of this 25 kDa protein to
a single band on an overloaded silver-stained gel in ten days.
The crystallization conditions for this orthorhombic P2P1P1 crystal is
defined for the native protein.
My questions are:
Is the anomolous scattering (?) method using a synchrotron
dependent on the native data set already obtained?
Can all the data be collected on a single crystal? Is a second derivative necessary?
Would this process be more difficult than the standard methods?
Does the difficulty depend on the number of Met in the protein?
AND: Is it feasible to do?
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