Dear all,
Is it possible to remove all the close contacts from the PDB structure in
coot.
Please suggest
--
WITH REGARDS
Rohit Kumar Singh
Lab. no. 430,
P.I. Dr. S. Gourinath,
School of Life Sciences,
Jawaharlal Nehru University
New Delhi -110067
Hi Jacob
If you look at SGs P312 and P321in ITC-A you'll see that they are quite
different in terms of the arrangement of the a.u.s relative to the symmetry
axes. So essentially the 1's are there to distinguish these. The extra 1
or 2 after the 3 of course signifies a screw axis. Note that for a
Hi JK,
we recently worked on a crystal with similar symmetry and I would recommend
you to read the two papers listed below. If you visually do see the "weak"
reflections, the space group is primitive orthorhombic (and not
body-centered orthorhombic). The strong Patterson peak at ~0.5, ~0.5, ~0.5
r
Dear Crystallographers,
I don't understand what the 1's are doing in space group names like P3212 or
P3112--can someone fill me in? Not easy to google this one.
JPK
***
Jacob Pearson Keller, PhD
Looger Lab/HHMI Janelia Research Campus
19700 Helix Dr, Ashb
We have data at ~3.2 A for a crystal that looked clearly like primitive
orthorhombic while indexing in HKL2000 (or Mosflm). Based on the systematic
absences I called it P212121 during scaling. However, we are having some
unexpected issues with finding a Mol. Rep. solution using a model that is
pres
Dear All,
I'd like to call your attention to a position announcement for a PhD level
structural biologist to join a new biotechnology company called HarkerBIO. I
am posting this announcement for any members of the CCP4 board that may be
looking for positions but please note that I am not invol
Dear Cosmo,
you may calculate effective resolution of your data set along different
directions using the program EFRESOL (article in press in J.Appl.Cryst., the
method is described by Urzhumtseva et al., 2013, Acta Cryst D69, 1921-1934).
You can download the program from
http://www-ibmc.u-stra
Hello All,
I've noticed that the figure-of-merit (FOM) and weighted difference map
coefficients (e.g. DELFWT) for the test set (FreeR_flag = 0) of reflexions
in an MTZ file as produced by a certain well-known ML refinement program
are all zero, while the same coefficients produced by another well-
Thank you, everyone!
Francesca
From: Enrico Stura [est...@cea.fr]
Sent: Tuesday, February 17, 2015 3:00 AM
To: CCP4BB@jiscmail.ac.uk; Mattiroli,Francesca
Subject: Re: [ccp4bb] how to reduce protein solubility
Francesca,
The most common failure is to have
Hi all,
I have a anisotropic crystal with cell dimensions of 78, 78 & 345. Is there a
method for quantitatively measuring the the anisotropy of my diffraction data
and a way to compare my data to that of similarly anisotropic crystals?
-Cosmo
Potentially there is more information in the 4 parameters HLA HLB HLC HLD
which can describe a bi-modal distribution of phase probabilities( that
would be generated by experimental phasing) than can be carried by the 2
parameter PHI FOM which will describe a uni-modal distribution. However if
HLC=
I am pleased to announce the publication of the latest issue of the
Computational Crystallography Newsletter:
http://www.phenix-online.org/newsletter/
A listing of the articles and short communications is given below.
Please note that the newsletter accepts articles of a general nature
of
20th ANNIVERSARY SCSB Structural Biology Symposium
You and your colleagues are cordially invited to join us for the20th
Anniversary Structural Biology Symposium to be held at Levin Hall on the
University of Texas Medical Branch Campus on beautiful Galveston Island
Dear colleagues
I have an MRC-funded PhD position currently available in my lab to study
proteins involved in sporulation of the human pathogen Clostridium difficile
(details below).
I would appreciate if you can pass the information to potential students and/or
advertise it in your institution
Dear all,
The version of Refmac that I currently use through ccp4i has "If following
features are found in coordinate file then make restraints to maintain them:"
activated by default for cis-peptides.
I usually deactivate it during refinement, but this means that if one does
nothing and moving
Francesca,
The most common failure is to have an excessive amount of salt (salting
in/ salting out), glycerol or other solubilizing
ingredient in your protein solution. I would suggest that you change the
pH and reduce the salt in your protein solution,
by microdialysis if you do not have mu
Just a possibility for salvage of your already set-up drops:
You can spike the reservoirs with some highly concentrated precipitant (no
matter what as long as
it sucks more water out of your drop). It does not solve your problem but
maybe you can
revive a few drops and get more information f
Dear all
In a few places (Refmac and Phenix, maybe there are also others), there is an
option to use either phase/FOM or HL for refinement and DM. Is there any
difference between these two? The dataset in question is a Fe SAD dataset.
Thanks.
Mohamed
Hi Francesca,
You could try using reductive methylation, this has always lead to a loss of
solubility (and protein!) in my experience. Jena bioscience and Hampton
research sell kits.
Best regards,
Paul..
[EvotecLogoMail]
Paul A. McEwan Ph.D.
Principal Scientist, Structural Biology
+44. (0)1235
Hi Francesca,
Try some zinc (1mM + ) in your protein buffer? Zinc tends to make a lot of
things less soluble in my hands.
Dave
On Tue, 17 Feb 2015 04:34 Mattiroli,Francesca <
francesca.mattir...@colostate.edu> wrote:
> Hi all,
>
> I am struggling with a protein complex that is too soluble. I h
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