Bioptix is another option you may consider for your needs. if they still
have the Bioptix Innovators program running you may also be able to have
the instrument placed for a free timed trial with training to see if fits
your needs. contact them to see. the sensor chips, one for amine-coupling
is
i wonder if crushing with a hammer maybe a good first step. does
streak seeding after that give smaller crystals amongst the range of
different size crystals possible. perhaps? either way would be good
for the summer student to try out.
--
Karthik
On Tue, Jul 26, 2011 at 10:55 AM, James Holton
Hi, I was looking around for programs that display space group symmetry
information and could not find any but perhaps i am lost for valuable or
relevant keywords.
I found two references TABLES and CRYST, but are there other alternatives
that are more recent, or that can run on more common
It makes slight sense if the word 'respect' can be correlated with whether
the drop is mixed (protein+ppt). i have heard some protein may indeed
crystallize if it were not mixed or vice-versa (do not expect it with
lysozyme though). it would make sense if diffusion played a role but with
few ul
Hi, I apologize immediately that this question is not directly related to
crystallography but the protein i am trying to overexpress is eventually for
that purpose. i understand the huge knowledge-base of people here
experienced in protein expression/purification and would appreciate any
insight
your story may be
different, but I agree that overexpression can indeed do weird things to the
guts of E. coli.
-James Holton
MAD Scientist
Karthik S wrote:
Hi, I apologize immediately that this question is not directly related to
crystallography but the protein i am trying
Hi Katja,
If your protein preparation did have salt, you could try lowering that salt
(if your protein tolerates) and grid search with varying (increasing) PEG
concentrations.
Seeding and Additives should really help. the effect/outcome is difficult to
predict but these two techniques are helpful
You know the sequence of the target so the missing residues can be built by
looking at the difference density. if the protein is phased right by MR then
the extra residues if they were actually present (and not clipped off in
crystallization) you should see them. coot can be used to visualize and
This link was posted earlier, perhaps it is the one you were looking for:
http://skuld.bmsc.washington.edu/scatter/AS_form.html
http://skuld.bmsc.washington.edu/scatter/AS_form.html--
Karthik
Graduate Student
University of Michigan
On Sat, Oct 31, 2009 at 10:44 AM, james09 pruza
I have been there, and like most things that we want to learn the best way
is to practice them. suggest joining a lab that solves structures using
crystallography would be your best way to learn. there are introductory
textbooks that will also give you a feel for the subject (like
crystallography
I have not heard of anyone checking for suitable cryo in that fashion how
fast can you do it before it is affected by room temp and how would you know
about the ice rings, but when you have crystal(s) and not crystal you can
freeze different ones in several different cryos (sugars, glycerol etc)
How is the solvent mask handled for zero occupancy atoms? In general is it
justified that i fear some of the electron density belonging to the protein
in the periphery of the molecule can be solvent flattened and i never see
them thereafter in my electron density maps or is this just not going to
...@umich.edu
_
On Thu, Sep 17, 2009 at 2:28 PM, Karthik S biokart...@gmail.com wrote:
How is the solvent mask handled for zero occupancy atoms?
In general is it justified that i fear some of the electron density belonging
to the protein in the periphery of the molecule can
You may be able to optimize them but that is still a step further, with
recent advances in microbeam at the synchrotron, you *may* be able to scan
through different regions of your crystal (especially if the stacking is not
exactly one on top and is little oblique) and collect data!
--
Karthik
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