Also, saying that you have 
a. 4.0 data  without defining the beam line
b. plates without defining the dimensions 
is of limited use to get feedback, in my view.

If you got 4.0 data at home, and your plates are at least a couple of micron thick,
 one of the few modern micro crystal beam lines is very likely to yield excellent data for you.

A.


On Oct 16, 2012, at 9:37, Tim Gruene wrote:

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Dear Jahan,

is your diffraction useless, or do you call 4A resolution useless? 4A is
not too bad and can be a start for structure determination while you are
waiting for better crystals.

You give very little information about what you actually have done, and
if you search the bb-archive for "how to get better crystals" you can
probably make a book from the number of hits.

If you got a large number of crystals while seeding, try harder - the
idea of micro seeding is to adjust the conditions below nucleation
concentration and seed there. Dilute your cat whisker further until you
have only very few seeds left (you may want to have a look at Fig.
11.2.(a) on p. 63 of http://shelx.uni-ac.gwdg.de/~tg/thesis.pdf to get
an idea of the effect.

If all else fails, you can also try restricted proteolysis, although I
would put this in "routine optimization methods" nowadays.

Good luck,
Tim

On 10/16/2012 12:01 AM, Jahan Alikhajeh wrote:
Dear Friends,

I am trying to crystalize a 70 kDa nasty protein but I got plate
shape crystals with high mosaicity and useless diffraction (up to
4A). I tried to improve/optimize crystallization but either I got
the same or nothing. I tried seeding but I had so many crystals
without any improvement. Does anyone have better idea than routine
optimization method in the lab? Thanks in advance.

Jahan


- --
- --
Dr Tim Gruene
Institut fuer anorganische Chemie
Tammannstr. 4
D-37077 Goettingen

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