-BEGIN PGP SIGNED MESSAGE-
Hash: SHA1
Dear Rhys,
with good 2.0A data you could try S-SAD, or MR-SAD. For the latter I
recommend autorickshaw (http://www.embl-hamburg.de/Auto-Rickshaw/).
Best,
Tim
On 10/01/2012 09:26 PM, RHYS GRINTER wrote:
Hi All,
I'm currently working on solving
Dear all,
The MX beamline at the Alba Synchrotron (Barcelona), BL13-XALOC, is now open
for user proposal applications. Worldwide institutes are eligible for
beamtime, which is established based on the peer-reviewed proposals. The
beamline is included in the Biostruct-X
It is with great sadness that I would like to inform the crystallographic
community of the death of one of the great pioneers of the field, Professor
Dame Louise Johnson.
Those of us who had the privilege to work alongside her benefitted greatly from
her vision for extending technique and
Physical Biochemist/Biophysicist
The Biochemistry and Cellular and Molecular Biology Department (BCMB) at the
University of Tennessee at Knoxville (UTK) is soliciting applications for a
full-time, tenure-track position at the rank of ASSISTANT PROFESSOR, to begin
August 1, 2013. The BCMB
Thanks for your help everyone!
It seems that the Balbes pipeline, followed by density modification in Phenix
has done the trick
Rhys
That's good to know, Rhys.
But would you mind sharing why did it work with Balbes? Is there a big change
in the position of the domains as related to your first searching model, or
huge loops that had been removed?
Carlos
Em 02/10/2012, às 14:42, RHYS GRINTER escreveu:
Thanks for your
Hi all,
I am using Phaser 2.5.1 for molecular replacement. I like to keep
tightly bound water molecules (HOH) in the input pdb file.
Phaser 2.1.4 outputs all HOH lines in the input pdb file to the output
pdb file, but Phaser 2.5.1 doesnot.
I am wondering if there is any way to carry input HOH
As a deliberate choice, we changed Phaser so that it would omit all HETATM
records from the model used for molecular replacement. This was largely
because when extensive water structure was carried along, it could mess up the
molecular replacement calculation. However, if you want something
Hi Randy
When you say carried along are you saying that they are used as part of the
molecular replacement search? Or are they temporarily put aside and them simply
added to the PDB in frame with the molecular replacement solution (but are not
part of the weighted structure factors output in
Hi,
I meant to say that they're included as part of the model for structure factor
calculation and in the output PDB file.
Best wishes,
Randy
On 2 Oct 2012, at 16:05, Francis E Reyes wrote:
Hi Randy
When you say carried along are you saying that they are used as part of the
molecular
Dear Randy,
I just noticed that Phaser 2.5.1 sets the occupancies of attached sugers
e.g. NAG, NAM etc. to zero, which caused Buster to crash. Resetting the
occupancies to one solved the problem, but other refinement programs may
not crash and may cause people unknowingly carrying on zero
I am assuming you are after something like a difference map of the two
surfaces.
http://www.pymolwiki.org/index.php/Map_set
Map_set command can average, copy, difference, maximum, minimum, sum and unique
Hope this is what you are after.
Dan
-BEGIN PGP SIGNED MESSAGE-
Hash: SHA1
Dear Koji,
in case that suits your needs you could do a superposition of the
input model (including HETATM) onto the output model. This would move
the HETATM's in place. By then deleting the model and merging HETATM's
with the output model (e.g. in
This indeed is sad news for today.
I just wanted to note that Professor Johnson's early papers on
time-resolved crystallography truly inspired me to continue in
crystallography, influenced my decision for my first postdoctoral position
and to push the limits. I still have the carefully
What a great lady to have inspired so many, and to remind us how welcoming
the field of X-ray crystallography has been in general for women because of
people like Dr. Johnson, Dorothy Hodgkin, and Rosalind Franklin, and many
others.
On Tue, Oct 2, 2012 at 12:03 PM, Gloria Borgstahl
As a devoted reader of the Protein Crystallography - the first and only
comprehensive manual of the protein crystallography,
I express my deep sorrow on the departure from us of DBE Commander, Professor
Louise Johnson.
May her soul rest in peace.
In full honor,
Dr Felix Frolow
Professor of
Dear all
I have off topic questions.
Why can't electrons continuously circulate the ring at synchrotrons instead
being refilled every few hours? Does new electrons injected into the ring
affect MX data collection?
Secondly, is it impossible to have all MX beamlines with insertion device as
Good questions!
I have off topic questions.
Not exactly off topic.
Why can't electrons continuously circulate the ring at synchrotrons
instead being refilled every few hours?
The electrons are traveling in pretty small packets. Eventually they get
too close to one another, and they
On 10/03/2012 12:09 AM, Christopher Browning wrote:
Dear All,
I was wondering if anybody knows how one can have two transparent
surfaces overlapping but then being able to see how the 2 intersect
using PYMOL. At the moment, if I have two transparent surfaces
overlapping I don't see how they
Try changing the transparency setting to Multi-Layer -- this will prevent the
2nd overlapping surface from appearing solid (assuming I understand you
correctly)
In the PyMOL menu bar, go to: Setting Surface Multi-Layer
Hope that helps!
Kip
On Oct 2, 2012, at 11:09 AM, Christopher
Hi Faisal,
There is no such thing as the ideal deviation from ideal geometry. As long as
your rmsZ values are below 1 (which they are), it's okay. Note that, in
contrast to popular belief, rmsd has no useful meaning for bonds and angles.
Genarally, rmsZ goes down with resolution but the
21 matches
Mail list logo
