Same here on El Capitan 10.11.6.
Mutate & Auto Fit still works though, but Simple Mutate crashes.
Mark J van Raaij
CNB-CSIC
www.cnb.csic.es/~mjvanraaijOn 23 Nov 2016 16:57, Julian Nomme
wrote:
>
> Same here on masOS Sierra...
> Julian
>
> Le 11/23/16 4:55 PM, Isupov, Michail a écrit :
> > Hi,
Hi Ivan,
Being in the same boat, I have investigated a bit. It seems to be a straight trade-off between more processing power, more RAM and less partability Macbook, Macbook Air, 13" Macbook Pro, 15" Macbook Pro.
For running Rosetta I think you will be thankful for the faster processors and extra
the same as the 1 in P1 ;-)
seriously, if you look at space group names:
143 P3
144 P31
145 P32
149 P312
151 P3112
153 P3212
150 P321
152 P3121
154 P3221
the 1s in 149 to 154 are necessary to differentiate them all.
On 18 Feb 2015, at 04:51, Keller, Jacob wrote:
> Dear Crystallograp
In our structures 1H6W (1.9Å) and 1OCY (1.5Å) we observed something similar, I
suspect the domain that makes the crystal contacts is three-fold disordered,
leading to layers of nothing. In our paper in JMB 314, 1137 (doi
10.1006/jmbi.2000.5204) we tried to explain it a bit, and describe what was
sure, "whether the structure can be solved" is a good criterion.
but often, when trying different heavy atoms, the structure can NOT be solved,
and then some criterion to judge whether to continue to try and solve it with
that data, or whether to focus on other datasets, other derivatives, anothe
Or perhaps there is only 1 copy and more solvent than you expect? This is not
that uncommon.
On 20 Sep 2014 12:09, Randy Read wrote:
>
> Just to add to what Herman said:
>
> The statistics are good for placing the domain represented by ensemble 1
> (TFZ=14.3) and the first copy of the domain r
same happened to me yesterday evening, but when I retried this morning, the
update installed fine.
Did not change anything in between.
On 14 Jun 2014, at 11:21, Felix Frolow wrote:
> CCP4BB list,
> Today I tried to install update 018, however I have lost the ability to do it
> from the GUI. Men
As the excellent tips that you got indicate, lower R-factors can be obtained by
getting better data (better crystals, better data collection, better data
processing) or better fitting, i.e. refinement. In this respect, I am impressed
by the automatic data processing protocols now being implement
turns out some people indeed have better memory than me:
WASP inside STAN server
http://xray.bmc.uu.se/cgi-bin/gerard/rama_server.pl
thanks!
On 14 Feb 2014, at 12:49, Mark van Raaij wrote:
> In the past I remember using a simple program or webserver to check whether
> modelled water mol
In the past I remember using a simple program or webserver to check whether
modelled water molecules might be metal ions, especially sodium, magnesium etc.
as they do not differ much in density to waters. Based on coordination.
However, I can't remember the name and can't find it in google or the
Well, like Folmer says, you don't have to withdraw the entry, you could just
let it be released before the paper is accepted. While in some projects there
may be a legitimate fear that other scientists use your unpublished entry for
things you don't want them to, in many projects this doesn't ma
Usually the skin is precipitated protein when it comes into contact with air.
In this case, avoiding contact with air may be the only way to avoid the skin,
i.e. crystallise using a technique that is not vapour diffusion, but for
instance microbatch, microdialysis or free interface diffusion.
O
the differences are likely to be on the protein surface, and these would make
the crystal contacts, i.e. it would be unlikely the protein could crystallise
in the same crystal habit.
Never say never in crystallisation (i.e. try anything), but I would go for
other things first like additives, dif
Dear Brett,
We have seen this behaviour several times for different adenovirus fibre head
proteins and don't really have an explanation for it. We have always set the
peaks up separately when we had enough protein.
For this purification, as you don't have enough protein to pool them
separately,
but it
> would be another way of looking at it).
>
> >>> Mark van Raaij 11/01/13 7:39 PM >>>
> the limit of 2000 reflections I guess is just because it would be a waste to
> "throw away" more reflections for refinement, once the statistical minim
Even if you remove the authors it is often easy to ascertain who they are by
reading the paper and reference list.
Marco Lolicato wrote:
>Hi scientists,
>this interesting topic brought back to my mind a similar discussion I had with
>a colleague of mine and now I want to share it with you guy
Dear Mahesh,
from the images you showed a few days ago I am not convinced the issue is
twinning, just overlaps due to the long c-axis. But of course, I do not have
have as much info as you, just those images.
Unless you are really convinced you have twinning, if you can see what you want
to see
PS For future data collections, try to get the long c-axis roughly along the
crystal rotation axis if possible.
On 16 Aug 2013, at 16:38, Mahesh Lingaraju wrote:
> Hi CCP4 folks
>
> I have a data set which is looks twinned ( see the image-1 - I zoomed on to
> the image so that one can spot t
doesn't necessarily looked twinned to me.
Rather it looks like you have a trigonal or hexagonal cell with a long c-axis.
On image 2 it seems you may have systematic absences along l, although it is
hard to tell the order. Perhaps P31, P32, P62, P64 or spacegroups with these
symmetries plus 2-fold
Well, if you do NMR you avoid the possible bottlenecks of having to obtain
well-diffracting crystals, and having to phase the protein (i.e. obtain SeMet
protein crystals or suitable heavy atom derivatives; or a suitable MR model).
But instead, you'll need to prepare labelled protein (15N and/or 1
i.e. the next program will be Graceless or Feckless?
On 2 May 2013, at 12:10, Phil Evans wrote:
> Reference:
> Gibbons, S. (1932) Cold Comfort Farm, Longmans, London
>
> On 2 May 2013, at 11:07, Roberto Battistutta
> wrote:
>
>> Hi everyone,
>> just a curiosity, why the name "aimless" for the
and 2VAK...average Bs for the twelve, sequence identical, chains vary from 28
to 53.
On 29 Apr 2013, at 22:09, David Schuller wrote:
> On 04/29/13 12:26, Roger Rowlett wrote:
>> FYI, I do know of one example of a solved structure where some of the
>> molecules in the ASU are poorly defined. In
reminds me of structure 1NEU, although here the gelation was reversible, see
ref and abstract below - the paper has a photo of a tube of soluble protein and
gelled protein
we have also had a couple of cold-sensitive proteins in our hands, that
precipitated at 4 degrees when concentrated, but we
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