Dear all,
Is there a way to specify (somewhat arbitrarily) a origin for any
molecular replacement package (in a polar space group) without
resorting to phased translation so that one could more easily compare
results from different MR runs?
Thanks,
Shao-Yang
--
Shao-Yang Ku
EIPOD Post
From your description, the protein concentration dropped from 10mg/mL
to 1-2mg/mL after freeze-thaw. It's hard to imagine that your protein
has been degraded. Degraded by what (protease)? At -80oC? Did you see
a ladder of lower bands on the gel after the freeze-thaw?
If you're interested
Quoting Bernhard Rupp b...@ruppweb.org:
I suppose most have read the Acta D editorial already
http://journals.iucr.org/d/issues/2010/01/00/me0408/me0408.pdf
but it seems another creative way of structure generation
has been discovered by some small molecule people:
?
Thanks alot already in advance for your help.
Sincerely,
Christopher
--
Shao-Yang Ku
EIPOD Post-doctoral fellow
Schneider Group
EMBL c/o DESY
Notkestr. 85
22603 Hamburgphone: 0049-(0)40-89902-160
Germany email: s...@embl-hamburg.de
Can you put a 6His-tag on your protein and add some Ni-NTA beads to
your solution to capture (and concentrate) the properly folded
molecules?
Quoting Xuan Yang pattisy...@gmail.com:
Dear All,
I am working on protein refolding via dialysis in large volumn
(typically 2~4 litters). It was
Hi Amit,
I wouldn't worry about acetate depleting the Sm3+. I have tried to
make a derivative of a kinase by soaking ions of lanthanoid series but
in the presence of phosphate buffer and ADP. In this case, lanthanoid
ions are *known* to precipitate with phosphate (and phosphoryl
moiety).