Dear all,
Please see attachment for a structural biology job advert in the lab of
Professor Dale Wigley at Imperial College.
Closing date for applications is 10th March.
For informal enquiries please contact Professor Dale Wigley
(d.wig...@imperial.ac.uk)
Cheers, Martin
HM2017001
Thank you Randy and Pavel for correcting my failure to find an
appropriate tool in my mental toolbox. I was thinking too much
in terms of examining a difference map rather than a performing
a resolution-dependent analysis of Fo;Fc agreement.
Is there a straight-forward way to extract what Hunter
Randy,
Use of correlation makes normalization superfluous, but as you say it
cannot distinguish from the causes of deviation which may not just be
missing density.
Pavel,
Thanks for the reference. Will look at it more closely.
But how is the error being separated into separate error components
Hi,
Is there a straight-forward way to estimate the amount of missing electron
> density that a particular protein structure is missing based on the
> difference between Fo and Fc?
>
Any refinement or map calculation software that uses likelihood-based
approach does this routinely. In
Hi,
I rarely disagree with Ethan, but there are in fact ways of getting some idea
of how much of the ordered structure from your crystal is missing in your
model. It's not based on the difference between Fo and Fc but rather more on
the correlation between them and how that varies as a
This is a good point, the difference between Fo and Fc can be great if Fc is
actually missing (an 'incomplete' structure). And of course this wreaks havok
in defining the maskf for bulk solvent, and refinement, etc. Incomplete can be
missing whole parts of the protein (say in model building) or
Dear All,
Please find details below for a PDRA position available at the University of
Leeds. Please note the deadline for applications is 21st March 2017.
The full candidate brief can be downloaded from the following web address:
https://jobs.leeds.ac.uk/FBSMB1100
To apply for the position
like others I'm not clear why you care where your protein runs on SDS-PAGE. I
think the band you're seeing is in fact the tetramer, suggesting your protein
(like KcsA) is very stable. Helical membrane proteins often migrate faster than
expected (by their Mw) on SDS-PAGE.
Also, never boil
