Dear Jerry, 

 

First of all, it will be hard to reproduce the conditions with the
glycosylated protein because by its nature, it is heterogeneous. One
thing I would try with the glycosylated protein is a detergent screen,
or if you don't have one, use a few NDSB's. Second, I would try setting
up a lower PEG condition concentration and seed into it with the phase
separated material, or with polystyrene nanobeads. Third, I would try
FID (Free Interface Diffusion- like Microlytic's Crystal Former-
www.microlytic.com) experiments, or use Enrico Sturza's technique with
the Granada (?) Crystallization Boxes. Have you tried shifts in
temperature? Start by warming up the protein to between 37-42C, then set
up the drops. Allow the plate to equilibrate at some temperature between
37-20C then transfer to 4C after 24H.

 

Something I suggest is that you go back to construct design and mutate
the amino acids being  glycosylated to something like GLY or ALA. If you
can, express the protein in a different system (if you used Ecoli, try
Insect cells or vice-versa). Alternately, you can use SGC's method of
dilute protease mixed with your protein prior to setting up the drops. I
have tried 1:10000 dilution, but I think that is too weak. I would start
with 1:100 or so. 

 

Good Luck, and let us know how it turns out. 

 

Regards, 

Bryan Prince.

 

 

 

 

From: CCP4 bulletin board [mailto:[email protected]] On Behalf Of
Jerry McCully
Sent: Wednesday, March 03, 2010 10:59 AM
To: [email protected]
Subject: [ccp4bb] crystallization of highly-glycosylated protein
complex-avoid phase separation

 

Dear ALL:

     Recently we've been trying hard to crystallize a highly
glycosylated protein complex ( 30% percent of carbohydrate in the total
120KD molecular weight). 

   IT is a high affinity protein complex. One component can be
crystallized in high salt condition and the other can be crystallized in
PEG.  

Through screening, we happened to get some very ugly crystals in PEG
condition using gel-fil purified complex sample. 

The problem is that it is very hard to repeat the screening condition.
In contrast, it is very 
easy to get phase separation in the drop although we tried to optimize
the protein and precipitant concentration. 

  We tried to de-glycosylated using PNGase and EndoH but failed in
non-denaturing condition.

Hampton additive screen  did not help either. We tried seeding several
times but so far we have not got any better luck.

  Can anyone give some guidance here? Thanks a lot,

Jerry McCully



   

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