Dear CCP4 community,
I am posting to get your suggestions on a Mac Pro system for structural
biology and not entertainment. Any comments will be appreciated. Please
feel free to send off line messages if you prefer.
My target is a Mac Pro with 8-12 cores and Dual AMD FirePro D700 GPUs. I
will r
Hi Afshan,
You mention:
The protein prep is same which was using to get the Hits.
So how old is your prep ? Was it stored at 4C or in LN2? Do you know if your
protein is stable under the conditions you stored it ?
How long after purification did it take you to get those crystals ?
How old is
Hi Afshan,
Have look at http://www.douglas.co.uk/Scaling_Up.htm, Patrick has some
general tips on scaling up. Elsewhere on his site you'll find tips for
conversion to microbatch, you may want to try that out as well. I assume
the screen crystals were not big enough to mount?
Flip
Op 4/16/20
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Dear Afshan,
- - Can you reproduce the crystals in the Linbro plates with the
identical solution used for the screening plate?
- - Did you compare the composition of the Linbro plate vs. the
screening plate?
- - Did you check e.g. the pH of the origin
Dear All,
I have encountered one problem to optimization the crystallization condition
manually. Actually i got the good shape and even size crystal in a screening
plate.
The condition are :
20% PEG 6000, 0.1M MES pH 6.0 whereas protein in 10mM Na-acetate pH 5.7 contain
50mM NaCl, 1mM EDTA &5
Lei,
1. Consider making the complex and then purifying the excess peptide
away by dialysis (size exclusion may be tricky since complex may be
diluted in the process).
2. Conventional wisdom would be to try to minimize the amount of excess
peptide as it may "interfere with crystallization". But c
Hello everyone
first I want to thank you guys in advance. I am trying to co-crystallize a 12
KDa protein with a 2 KDa peptide. The biochemistry studies showed the binding
should be 1:1 . but the binding is not very strong ( Kd is around 20-40 uM). I
am wondering, is there any bad effect of e
