Janssen Research & Development, L.L.C., a division of Johnson & Johnson's
Family of Companies is recruiting for a Scientist, Structural Biology,
located in San Diego, CA.
At the Janssen Pharmaceutical Companies of Johnson & Johnson, we are
working to create a world without disease. Transforming
*Scientist, X-ray Crystallography - San Diego, CA*
Pharmaceuticals
*Job Description *
Janssen Research & Development, L.L.C., a division of Johnson & Johnson's
Family of Companies is recruiting for a Scientist, X-ray Crystallography,
located in La Jolla, CA!
At the Janssen Pharmaceutical
*Scientist, X-ray Crystallography - San Diego, CA*
Pharmaceuticals
*Job Description *
Janssen Research & Development, L.L.C., a division of Johnson & Johnson's
Family of Companies is recruiting for a Scientist, X-ray Crystallography,
located in La Jolla, CA!
At the Janssen Pharmaceutical
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refinement, it's ok and Rfree is 52%. Does that mean the
solution might not be correct? What's the acceptable Rfree for the initial
refinement? Thanks a lot.
Rui
Does anyone know a good way to search for a fragment matches(~16 residue
long helix or loop) from pdb?I have a fragment of pdb and want to pull out
all the similar structures from the pdb, any easy way to do that? Thanks a
lot.
On Tue, Oct 30, 2012 at 9:34 AM, David Briggs
. Does
anyone know why? Thanks a bunch.
Rui
wonder how feasible
it is to do modeling in laptop. Sorry for the dumb question, but I just want
to get a sense how fast it should be, so that I can have things fixed.
THanks.
Rui
Hi, All,
We are trying to crystallize a protein and found some initial hit in the
following conditions,
pH 4.8, 0.2 M AS or some other salts ( NaCl,LiCl, MgCl2 ), 32% PEG4000 or
PEG3350 ). However the quality of the crystal is not so great,some of them
look like needle cluster(very long in
Hi, All,
I have a general question for refinement. I tried to refine a dataset that
is about 2.3A and got R/Rfree is about o.18/0.24. RMS(angles): 0.77,
RMS(bonds): 0.003
however, when I check with molprobity, There are still some outliers and
some bad contact that is overlap 0.4 A.
Hi, All,
I tried to use phenix to add water molecules, and when I check those waters
in coot, I can easily delete them if they are not in right spot. However, if
I see some clear positive maps that seems like water, can I add manually at
that position? How to do this in coot?Or any other way?
Thank you all for the quick reply. Kim and Ingrid both pointed me to the
same direction!! Thanks a bunch :-)
On Thu, Dec 3, 2009 at 2:37 PM, Frederic VELLIEUX
frederic.velli...@orange.fr wrote:
Hi Rui,
I am at home so this is all from memory. In coot.
Use the control key (pressed down
Hi,
Is there any tutorial that describe the refinement procedure with refmac?
There are several options, restrained, rigid body, TLS...,I have a crystal
has 2 copies in ASU, and currently I'm just using restrained refinement, but
wonder if I should also try some other type of refinement too .
Hi,
I found this old post in ccp4 and it's very useful. I used the same
procedure Scott described to add a ligand into pdb file. What I did, is in
coot, search for the ligand in the library and find the ligand and then
merge. However, when I tried to refine in refmac, it has some problems, it
? At this moment, my
solution has the same number of residues as the template and it's hard to
see extra densities. Should I delete some residues before and after the loop
first then try to bring up the missing densities?Any suggestions would be
appreciated. Thanks.
Rui
Hi, All,
What's the general rules for selecting cryosolvent?I got crystals in 30%
PEG4000/PEG3350, 0.2M AS and 0.1M NaAC,how should I choose cryosolvent?
Thanks.
Rui
Dear All,
I have a peri domain protein that is stable in high salt concentration(500
mM), if I dialysis to a lower salt buffer and then concentrate, it'll
preticipate out. If I need to crystallize it, can I use the high salt
buffer? Is there any optimization kits that could help to increase the
the
number of residues are different and there might be gaps and insertions in
the alignment. Any suggestions of good programs?
Thanks.
Rui
to
ask is that with this type of plates, the reservoir buffer volume is 100 uL,
vs hanging drop with 600 uL, that will it be harder to get crystals?
On Fri, Apr 24, 2009 at 1:54 PM, Patrick Shaw Stewart patr...@douglas.co.uk
wrote:
Rui
Microbatch – which I take to mean crystallization under
Hi,
I have a question about the method for crystallization. With traditional
hanging drop(24 wells), one slide can also hold for multiple drops but it
requires the buffer quite a lot, 600uL? Microbatch can save buffers,only
100uL is required, and also can hold up to three samples in the sitting
Dear all,
I want to pull out the sugar binding proteins from the pdb, however, there
are so many different names for the ligand ( GAL, GLC, RIP... ) and it's not
easy to get a complete list. If I want to pull out some fragments based on a
specific geometry ( for instance, the glucose has C1 C2 C3
Hi, All
I have dozens of complex structures ( protein + ligand ) and want to align
the structures based on the ligand. Does anyone know such kind of program?
Or if can get the information around the ligand site, that would be even
better.
Thanks.
R
Thanks for the answer. Actually, it's the opposite. I have many structures
that have different protein but with the same ligand(sugar). And I want to
fixed the ligand and align the different proteins to see the active site.
On Sun, Apr 12, 2009 at 7:36 PM, John Badger jbadg...@san.rr.com wrote:
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