Dear all,
We would encourage anyone interested in attending the 2024 CCP-EM/Diamond
Icknield workshop to apply soon, as we are fast approaching our maximum number
of applicants. For more information about the workshop and how to apply, see
below.
The 2024 CCP-EM/Diamond Icknield Workshop to
Dear Martin,
On Thu, Jun 13, 2024 at 10:40:43AM +0100, Martin Malý wrote:
> Thank you for the link. It would be great if https://proteindiffraction.org/
> (IRRMC) was rescued.
They are back in business since a couple of months now - at least
regarding new data appearing there.
> I preferred this
Dear all,
Please join the NIH supported CryoEM centers at our next CryoEM Current
Practices webinar.
Time: Thursday, June 27, 2024 at 9 AM pacific / 12 PM eastern time
Speaker: Dr. Keerthi Gottipati, Indiana University, Bloomington
Title: Cryo-EM structure of HIV-1 Rev Response Element RNA: Str
Dear John,
Please could you give us an advice who to contact - who presented in
Melbourne?
I think there are more of us who are not successful in contacting their
support.
Thank you.
Martin
On 13/06/2024 20:24, John R Helliwell wrote:
Dear Gerard,
Quite so. But, as this CCP4bb has also obser
Dear MartinHere is the weblink to our IUCr 2023 Committee on Data Workshop in Melbourne:-(IUCr) Melbourne Workshopiucr.orgPresentations are available for our speakers as you will see theirin . The IRRMC talk was given by Wladek Minor. I hope you can join us at IUCr 2026 Calgary as we progress this
This old message claims that / = "weighted" by s.
If counting error is significant, s will be larger for stronger reflections, which are likely to
have small I/s, so in general / > unweighted . As Werten points
out.
However this seems to be the opposite of the OP's situation, if both measur
OK, folks, the last day to voice your opinion on this is Monday June 17.
survey is here: https://www.research.net/r/P30_RFI
I encourage anyone who has used these synchrotrons to chime in. Your
opinion matters, but the NIH cannot read your mind! I personally think
it very important that they
Hi all,
I am wondering what the best practice is to compare datasets that are of the
same protein but different quality, for instance 2 vs. 3 A.
I know that truncating the structures to the same resolution bin is alright,
but the data quality in the lower resolution bins are also not the same
BNL NSLS-II, FMX or AMX beamlines: overall coordinator Vivian Stojanoff
Beamline scientists
FMX Wuxian Shi or Martin Fuchs or Alexei Soares
AMV Jean Jakoncic or Edwin Lazo or Dale Kreitler
Jeffrey B. Bonanno, Ph.D.
Department of Biochemistry
Albert Einstein College of Medicine
1300 Morris Park Av
Correction made below - AMV in my original message should read AMX of course
__
BNL NSLS-II, FMX or AMX beamlines: overall coordinator Vivian Stojanoff
Beamline scientists
FMX Wuxian Shi or Martin Fuchs or Alexei Soares
AMX Jean Jakoncic or Edwin Lazo or D
I should clarify. I am mostly concerned about the electron density map.
I want to make sure that I can most closely compare the maps from two
different quality structures, rather than the datasets themselves via CC1/2
or other metrics. This is more so for interpreting structural changes.
For ex
Hi Matt,
I guess that the datasets have the same spacegroup and very similar cell
parameters?
And that you have two similar models that you obtained by refining against the
datasets?
What you can do is to find out which dataset gives the better model, and is
therefore better
(i.e. generally
I seem to recall Wladek mentioning that he has been trying to keep
proteindiffraction.org alive using his own personal funds, which must be
difficult. The NIH grant for Proteindiffraction.org was U01 HG008424,
which had a Project End date of 2018-05-31, and no record of a renewal.
It was part
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