Hello Marc-
My first thought is do you have the correct space group? Are you searching for
other space groups in the point group? Second, helicases are multimers, but the
orientation of the monomers that make up the multimers may deviate
significantly. If you didn't use a monomer, it's worth do
Two other choices:
https://data.sbgrid.org/
https://proteindiffraction.org/
Best-
Todd
From: CCP4 bulletin board on behalf of JEROME JOHNSON
Sent: Wednesday, October 18, 2023 11:23 AM
To: CCP4BB@JISCMAIL.AC.UK
S
Certainly not trying to be insulting by the suggestions but could it be as
simple an alignment issue with the crystal, issues with the beam alignment or
crystal damage following a fluorescence scan? The cryo setup?
Like James, I’ve seen crystals decay quickly in high salts at longer
wavelength
I like cases like this as cautionary tails for the crystallography class. In
this case, the sequence is mismatch in several places, ex. residues 1165-1170
should be 1153-1158 which flows nicely after you add a residue to 1151. There
are other places where the mainchain has slid and is out of reg
Hello All-
I am overlaying a series of structures that have a similar sequences and the
same topology, and I would like to represent an illustration to shown
commonality or lack thereof across the surface of the protein. I am most
interested in surface, ie. differences in peaks and valleys. D
On a side note, I assume that you have searched with both P2 as well as P21 for
your space group. If not, I will point out that there are 265 submissions in
the rcsb for the P2 space group, compared to 20,698 for P21. That makes P2
fairly rare. Good Luck! - Todd
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