Frank,
you are asking me to remove features that I like, so I would feel that the
challenge is for you to prove that this is harmful however:
- at the minimum, I find it a useful check sum that the stats are internally
consistent (though I interpret it for lots of other reasons too)
- it is
Dear Frank,
You are forcefully arguing essentially that others are wrong if we feel an
existing statistic continues to be useful, and instead insist that it be
outlawed so that we may not make use of it, just in case someone misinterprets
it.
Very well
I do however express disquiet that we
Do you have an inactive variant of the protein? If yes, use limited
proteolysis in the presence of methylated histones to find out which
flexible parts are really important and or protected by complex
formation. Further, try to crystallize a complex of inactive demethylase
and methylated
Dear Colleagues
I would really appreciate if you could share the following info
regarding this available position.
Best regards and thanks
Kristina
We are looking for a highly motivated research technician to join the
collaborative project between Sascha Martens
I know that this might be considered heresy on a crystallography mailing list,
but do you have any friendly NMRists at your institution?
D
Dr David C Briggs
Hohenester Lab
Department of Life Sciences
Imperial College London
UK
http://about.me/david_briggs
Graeme, Andrew
Jacob is not arguing against an R-based statistic; he's pointing out
that leaving out the multiplicity-weighting is prehistoric (Diederichs &
Karplus published it 20 years ago!).
So indeed: Rmerge, Rpim and I/sigI give different information. As you say.
But no: Rmerge
>I do not see what harm there is reporting Rmerge, even if it is just used in
>the inner shell or just used to capture a flavour of the data set overall. I
>also appreciate that Rmeas converges to the same value for large multiplicity
Consider a callow young grad student, David, who being
Fab fragment binding towards long loop
在2017年07月04日 23:22，dongxiaofei 写道：
Dear ALL,
I want to make a protein crystal,but there is a long loop between domains of
protein , which contains two small domains owning about 40 amino acids
respectively and a loop about 70 amino acids.
Loop is so
I would like to support Graeme in his wish to retain Rmerge in Table 1,
essentially for exactly the same reasons.
I also strongly support Francis Reyes comment about the usefulness of Rmerge at
low resolution, and I would add to his list that it can also, in some
circumstances, be more
