I am serious about checking the anomalous map!!
(trivial from REFMAC - key word anom map on)
Then do a peak search and just check first that the rogue residue IS CYS
first - you should see the S as a peak..)
Eleanor
On Wed, 10 Jul 2019 at 07:38, Lumbini Yadav wrote:
> Thanks for the reply.
>
Thanks for the reply.
The distance between sulphur and centre of Fo-Fc map is around 2.5A. The
density does not appear to be of hydrogen (attached image) anisotropy
refinement also does not help.
On Tue, Jul 9, 2019 at 5:13 PM Anthony Addlagatta
wrote:
> Lumbini,
>
> It would useful to know th
Dear Jessica,
You can try http://manoraa.org for ligand interaction observation. This server
helps you to observe structural conservation environment of any ligand in the
PDB by clicking atoms versus PDB chains you want to superpose on. If you
classify HEME into different UNIPROT, you can see
The Northeastern Collaborative Access Team (NE-CAT), located at the Advanced
Photon Source at the Argonne National Laboratory in suburban Chicago, is
seeking applicants for a beamline scientist position. The primary
responsibilities of the staff scientist will be to provide user training and
su
Hard to see from a static image, but could it be an alternative
conformation?
Pavel
On Tue, Jul 9, 2019 at 2:32 AM Lumbini Yadav wrote:
> Dear all,
>
>
>
> We have found a huge Fo-Fc density close to cysteine residue (see attached
> image) in the structure with resolution of 1.2A. In the crystal
Refining B-aniso's will clean up a difference map at that resolution.
Sent from Yahoo Mail on Android
On Tue, 9 Jul 2019 at 16:57, Bonsor, Daniel wrote:
#yiv3128113039 #yiv3128113039 -- _filtered #yiv3128113039 {panose-1:2 4 5 3 5
4 6 3 2 4;} _filtered #yiv3128113039 {font-family:Calibri;
Dear CCP4 readers,
The Hauptman-Woodward Medical Research Institute has two current openings, one
as a synchrotron macromolecular crystallographer at the IMCA beamline in
Chicago, and announced today, for a cryo-EM center director based in Buffalo
NY. Both will have the opportunity to interact
Hi,
This is a reminder and additional details of an upcoming ‘Training Day’
organized by the
Biochemical Society.
Engineering recombinant proteins for structural and functional studies
Tentative venue: CIWEM, Saffron Hill, Holborn, London EC1N 8QS (near
Farringdon station)
Currently, fees a
Have you mass-speced the protein before crystallization to make sure it wasn’t
derivatized during expression and/or purification, or compared the mass spec of
the crystals verses purified protein? Any fancy reagents or other reductants
used during purification?
What about S-Acetyl-cysteine (3-le
Lumbini,
It would useful to know the distance between the sulfur and center of the Fo-Fc
map that you have shown. Since you have very high resolution data, the extra
density could be for a hydrogen atom in CSO-H (sufeneic acid) or anisotropy of
the oxygen atom.
Anthony
From: 176a9d5eba
Any anomalous diffraction?
On Tue, 9 Jul 2019 at 10:32, Lumbini Yadav wrote:
> Dear all,
>
>
>
> We have found a huge Fo-Fc density close to cysteine residue (see attached
> image) in the structure with resolution of 1.2A. In the crystallization
> condition, we have PEG 3350, Potassium phosphate
Dear all,
We have found a huge Fo-Fc density close to cysteine residue (see attached
image) in the structure with resolution of 1.2A. In the crystallization
condition, we have PEG 3350, Potassium phosphate monobasic, glycerol and
protein was in Tris and NaCl. Before freezing the crystals were so
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