It looks as if you have a and b about the same length. In that case indexing of
the patterns may randomly switch h and k. The CCP4 program Pointless (in ccp4i
Data reduction -> Symmetry, Scale, Merge (aimless) or Find or Match Laue
group). Give your 1st dataset as the reference.
Phil
On 30 Dec
Dear Dr.Evans,
Thanks for your reply.
The unit cell parameters are a=140 , b=110, c=44., Hence i am afraid, the
interchange couldn't have occurred due to similar a and b. I had performed
dehydration using PEG in the said case. I agree that dehydration or soaking
with ligand can hardly lead to
OK they looked similar in your pictures
Maybe you have two different crystal forms
Phil
On 30 Dec 2014, at 16:56, "" wrote:
> Dear Dr.Evans,
>
> Thanks for your reply.
>
> The unit cell parameters are a=140 , b=110, c=44., Hence i am afraid, the
> interchange couldn't have occurred due to
Hi,
I have difficulties to comprehend your description. I understand
- most crystals grow in P21212, with cell a=140 , b=110, c=44
- some crystals grow in P21212, with cell a=110 , b=140, c=44
Is that correct? If so, can you refine the structures? To what R-values, at
which resolution?
The sen
Translate it by 13 microns. And use enough attenuation to get 180
degrees at each position.
The track length of photoelectrons from 1 A X-rays in water, protein,
plastic, and other materials with density close to 1 g/cm^3 and atomic
numbers close to 7 is about 3 microns (Cole, Rad. Res. 1969)
>Yes, it gets complicated, doesn't it? This is why I generally recommend
trying to use a beam that matches your crystal size.
...or is bigger, right? Diffuse scattering, yes, but more even illumination
might be worth it?
Generally, James, I have a question: what is the nature of the intensity
Dear all
The protein that was crystallized is only the first 105 residues of a
230-residue protein. In the structure, I can see density for residues 6-72. For
deposition, should the whole native/biological sequence be deposited?
Thanks.
Mohamed
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Mohamed,
You always list the sequence of what's actually in the crystal, e.g. 1-105.
(Not: what's in the model or what the sequence of the full length protein is).
Make sure that if there's any lingering residues from any affinity/purification
tags they get included in the sequence too.
Phil
I would disagree. You list as sequence what you cloned and expressed. If you
are missing parts then you have to describe why e.g. Proteolysis or disordered
etc.
Best to actually do a mass spec analysis on those crystals since a significant
portion is missing.
Jūrgen
..
Jürg
Yes, bigger is okay, and perhaps a little better if you consider the
effects of beam/crystal vibration and two sharp-edged boundaries dancing
over each other. But bigger is better only to a point. That point is
when the illuminated area of non-good-stuff is about equal to the area
of the good
Several things, first your diagrams do not have the correct ratios of any unit
cell dimensions, so I am not sure why there is the distortion. But it is so,
and therefore not clear in any case which axis is which.
Second you didnt say how you solved the structures. - if it was by molecular
repl
Hello CCP4 users,
I am working with some DNA binding proteins. Can someone explain me how to
measure/calculate the bendability of a DNA molecule after binding to proteins
and foldabilty of protein molecule?
It will be good if you mention any reference(s).
Thanks in adv.
-Gajanan
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