near
to where you are looping your crystals to reduce evaporation of water from
your drop.
Good luck!
Liz
Quoting Mahesh Lingaraju mxl1...@psu.edu on Wed, 22 Jan 2014 12:28:15
-0500:
Hello folks,
I have crystals for a protein which form in 0.1 M MES pH 6-6.75, 10%
dioxane and 1.6
Hello folks,
I have crystals for a protein which form in 0.1 M MES pH 6-6.75, 10%
dioxane and 1.6-2 M Ammonium sulphate. Based on little experience I have
finding the right cryoprotection for salt based conditions; I have tried
glycerol (15-25%), Ethylene glycol (20-25%), DMSO (15-20%) and
with higher amounts. Very often crystals are much happier when you don't
soak/tinker with them and freeze them straight out of the drop.
Good luck.
Mark
-Original Message-
From: Mahesh Lingaraju mxl1...@psu.edu
To: CCP4BB CCP4BB@JISCMAIL.AC.UK
Sent: Wed, Jan 22, 2014 10:38 am
description of the random microseeding method*D'Arcy, Allan,
Frederic Villard, and May Marsh. An automated microseed matrix-screening
method for protein crystallization. Acta Crystallographica Section D:
Biological Crystallography 63, no. 4 (2007): 550-554.
On 17 January 2014 22:24, Mahesh
Thanks for the input folks. Ill surely try it. Hopefully some christmas/new
year miracles will happen.
Thanks again
Mahesh
Dear all,
I was wondering if it sounds logical to use the crystals from a possible
structural homolog as seeds to induce nucleation ? (in terms of overall
sequence,
Dear all,
I was wondering if it sounds logical to use the crystals from a possible
structural homolog as seeds to induce nucleation ? (in terms of overall
sequence, the proteins are considerably different but based on sequence
alignment and structures from other related proteins, it is highly
Hi All
On similar lines, I have been trying to optimize crystallization conditions
for my protein. Initially, I had showers of needles in a PEG screen which
did not really improve after screening around the condition. So, I seeded
these needles into all the screens that I have available and I
Hello experts
Thanks for your insights.
For one of the structures, it turned out to be a rendering issue by pymol
like matt pointed out. For the other, the residues are clearly in a less
than ideal position. Even if I see deviation from the RMSD plots, i cannot
be sure that the structure were
Hello Experts,
I was wondering if the R, Rfree, RMSD for bonds and angles calculated by
polygon plug in in PHENIX GUI using the cif file pdb file deposited in
protein structure database would be the same as reported in
database/publication ?
I apologize in advance if this is a PHENIX specific
Message-
From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of
Mahesh Lingaraju
Sent: Friday, October 11, 2013 21:59
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] R and R free from CIF file deposited in PDB
Hello Experts,
I was wondering if the R, Rfree, RMSD
converted to XDS now ? Welcome to the club.
Jürgen
On Aug 25, 2013, at 8:35 PM, Mahesh Lingaraju wrote:
Hello everyone,
I collected a dataset which looked like it is twinned ( or a really long
axis in the cell) and did not process in HKL2000 and MOSFLM but with some
of help
Hello everyone,
I collected a dataset which looked like it is twinned ( or a really long
axis in the cell) and did not process in HKL2000 and MOSFLM but with some
of help and suggestions from CCP4BB, XDS was able to process it. The data
looks good upto 1.7 Å. However, the rfree is stuck at 0.34
hello everyone
Can anyone point to me where i could obtain the programs twinabs, cell_now
? i cannot seem to locate them by simple googling.
Thanks
mahesh
i am not sure this would work as his protein seems to be degraded by the n
end degradation pathway. i feel like it almost needs to be expressed as a
fusion protein with some stabilizing sequence
On Fri, Aug 23, 2013 at 10:08 PM, Roger Rowlett rrowl...@colgate.eduwrote:
Why not adopt a
will get
a better quality of data with a more optimal strategy, but I would never
say never. If I had a penny every time people told me 'you cannot process
that'…
Petri
On Aug 19, 2013, at 11:40 PM, Mahesh Lingaraju mxl1...@psu.edu
wrote:
Thank you experts for your valuable suggestions. I
, Mahesh Lingaraju пишет:
Hi Jürgen
you are right, I did not try any major optimization yet. I only tried to
vary PEG and protein concentration. That did not really improve things too
much. The protein mostly forms spherulites beyond 25% PEG. I am also
thinking that these crystals are poorly
Thank you experts for your valuable suggestions. I think Ill try to solve
it by proper data collection strategy the next time as i am unable to
process my current data even with the tricks that were mentioned here.
Thanks again
Mahesh
On Fri, Aug 16, 2013 at 2:04 PM, Bosch, Juergen
Hello people
I recently obtained hexagonal rod like crystals (150x50x20 um) which turned
out to be non diffracting. What is the usual convention for cases like this
? do people usually give up on the condition or still try to optimize it ?
The crystals are also not very reproducible. I believe
, Mahesh Lingaraju mxl1...@psu.edu wrote:
Hello people
I recently obtained hexagonal rod like crystals (150x50x20 um) which
turned out to be non diffracting. What is the usual convention for cases
like this ? do people usually give up on the condition or still try to
optimize it ?
The crystals
On Aug 19, 2013, at 5:46 PM, Mahesh Lingaraju wrote:
Hi Petri
They are non-diffracting at the home source and they are cryo cooled. Like
david suggested I guess ill try introducing a buffer as my condition does
not have a buffer. it is ammonium acetate and PEG 3350.
Thanks for the encouragement
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