Most of the labs sharing our Phoenix have had enough trouble with exactly
this that our standard procedure is to now to use 1 µl drops (.5/.5
protein/well) in our initial screens those scale up much more reliably to
the 24-well format and seem less finicky in general, reducing the chances of
an
Hi Matt
Rajesh asked a similar question last week, below
Essentially, you have to *reduce *the protein concentration when you scale
up because you lose proportionally more protein from smaller drops.
This usually works very well and we see no reason to use more than 0.3 +
0.3 for initial
Dear All,
I have searched the archives and would like more information about
reproducing robot tray hits using 24-well hand trays. I reproducibly get
crystals when I use small volumes (0.5 ul) in 3-well intelliplates but only
precipitate in 1-2 ul sitting drops in 24-well hand plates.
What
I have seen people only use robot to optimize their crystal and get
good diffraction (~2 A). If you keep having trouble, you can try this
method instead, even though generally the case is the bigger the drop
the bigger crystal.
I remember the archive suggest us to use higher concentration of
On Mon, 2012-03-26 at 11:57 -0600, Matthew Lalonde wrote:
What parameters should I vary to reproduce crystals in hand plates?
First of all, protein concentration. It also does not hurt diluting
your reservoir since you are getting precipitates. If your goal is to
get bigger crystals (which is
Hi Matt,
This doesn't really answer your question directly, but sidesteps
around the issue -
I wrote a little something on this exact subject not so long ago -
http://xtaldave.wordpress.com/2012/02/23/on-protein-crystallisation/
(You can ignore the first 5 paragraphs of intro - it was written
