I posted this offline to Pavel, but maybe there are more people out there who
might find it useful?
Hi Pavel,
We have built and use See3, which is a replacement for CTweb that doesn't use
flash. It still uses the CM (Crystal) database. If you are interested you can
check it out (it would be a
Hi all,
Interesting discussion, and personally, I think Rasmus has hit the nail on the
head. Here is a challenge to the CCP4bb - can we make a list 10 female
developers of crystallographic software who would be appropriate invitees as
instructors to this course? (I can only think of 4)
Cheers,
Hi,
Another way of estimating a starting protein concentration is to watch your
concentration process β if your protein is in a spin concentrator (with an
appropriate membrane cutoff size say ~ [MW protein]/3) and is losing volume
really quickly then keep going. As soon as the concentration st
Hi,
To add to this thread, there are a few more easy things to try β
Try doing matrix microseeding and try doing limited proteolysis. Even though
the following link describes how we do this in our laboratory, (the C3 Facility
in Melbourne) the pages give a quick overview to both matrix microsee
And if you log in to C6 (c6.csiro.au - one can use the guest account: click on
"Or click here to try guest account") - navigate to "screens list"=>"commercial
screens" => KERAfast => and if you click on the screen then it will come up
with a description of what is in every well, and (most) of t
"I think my behaviour is in the allowed region, but others think I'm a right
out liar"
Janet Newman
Principal Scientist / Director, Collaborative Crystallisation Centre (C3)
CSIRO Material Science and Engineering
343 Royal Parade
Parkville. VIC. 3052
Australia
Tel +613 9662 7326
Email janet.new.
Interesting topic,
Certainly the two papers suggested by Georg are relevant, and I fully agree
with the comments from Daniel that it is hard to predict the behaviour of any
given protein from a statistical analysis of proteins in general.
I find it interesting that even with the use of incubato
There are a bunch of people doing this β in the small molecule world. And a lot
of work has been done on some very robust protein systems too. Can you guess
which ones?
The real issue (at the moment) is that all the pre-work needed to predict if or
how a protein might crystallise takes more wor
Throwing my hat in with Artem's here -
Not only is there limited funding for (biological) crystallisation, there is
perhaps even less interest.
Some of the reason is that what we do now works much of the time, so why
actually think about things when another screen (or another construct) might d
Hi Nemanja,
I have tried doing this, and it has never really worked for me, even with
careful rinsing with MilliQ water after washing, I could never get well-shaped
drops on a recycled plate. They are also a real pain to wash out, and itβs hard
to get the last traces of protein out of the subwe
I'm guessing quite big drops on a somewhat hydrophobic surface? Also guessing
that the protein foams quite a bit, and that there were 6 (or four) more or
less equal size bubbles that took up almost the whole drop when it was set up.
Bubbles tend to pack quite efficiently
(https://physicsworld.c
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