Hi Tassos, Tim, I wonder why would you or anyone on this list worry whether biological questions that can be asked and answered with structures are relevant to justify the resources? I think there is abundant evidence that this is the case. Unless your point is that crystallography is now dead for all practical purposes... then yes, I fully agree :-) It would however be wrong to erase its historical contribution to understanding biology.
Best wishes, Radu > I would wonder more if the biological questions you can *ask* with a (crystal) > structure are sufficiently relevant to justify the resources. > > Sent from my iPhone > >> On 15 Jul 2019, at 22:08, Tim Grüne <tim.gru...@univie.ac.at> wrote: >> >> Dear James, >> >> 10) are the biological questions that you can answer with a (crystal) >> structure sufficiently relevant to justify the resources? >> >> Best, >> Tim >> >> >> >> Am 15.07.2019 21:44, schrieb Holton, James M: >>> Hello folks, >>> I have the distinct honor of chairing the next Gordon Research >>> Conference on Diffraction Methods in Structural Biology (July 26-31 >>> 2020). This meeting will focus on the biggest challenges currently >>> faced by structural biologists, and I mean actual real-world >>> challenges. As much as possible, these challenges will take the form of >>> friendly competitions with defined parameters, data, a scoring system, >>> and "winners", to be established along with other unpublished results >>> only at the meeting, as is tradition at GRCs. >>> But what are the principle challenges in biological structure >>> determination today? I of course have my own ideas, but I feel like I'm >>> forgetting something. Obvious choices are: >>> 1) getting crystals to diffract better >>> 2) building models into low-resolution maps (after failing at #1) >>> 3) telling if a ligand is really there or not >>> 4) the phase problem (dealing with weak signal, twinning and >>> pseudotranslation) >>> 5) what does "resolution" really mean? >>> 6) why are macromolecular R factors so much higher than small-molecule >>> ones? >>> 7) what is the best way to process serial crystallography data? >>> 8) how should one deal with non-isomorphism in multi-crystal methods? >>> 9) what is the "structure" of something that won't sit still? >>> What am I missing? Is industry facing different problems than >>> academics? Are there specific challenges facing electron-based >>> techniques? If so, could the combined strength of all the world's >>> methods developers solve them? I'm interested in hearing the voice of >>> this community. On or off-list is fine. >>> -James Holton >>> MAD Scientist >>> ######################################################################## >>> To unsubscribe from the CCP4BB list, click the following link: >>> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1 >> >> -- >> -- >> Tim Gruene >> Head of the Centre for X-ray Structure Analysis >> Faculty of Chemistry >> University of Vienna >> >> Phone: +43-1-4277-70202 >> >> GPG Key ID = A46BEE1A >> >> ######################################################################## >> >> To unsubscribe from the CCP4BB list, click the following link: >> https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1 > > ######################################################################## > > To unsubscribe from the CCP4BB list, click the following link: > https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1 > -- Radu Aricescu MRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge Biomedical Campus Cambridge CB2 0QH, U.K. tel: +44-(0)1223-267049 fax: +44-(0)1223-268305 www: http://www2.mrc-lmb.cam.ac.uk/group-leaders/a-to-g/radu-aricescu ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1
