Dear Colleagues,

I would like to add my voice to those advocating making available raw
diffraction images and point out another resource for raw data deposition,
https://cxidb.org, particularly for the case of emerging methods such as
serial crystallography.

Cheers,
Filipe

On Thu, 19 Mar 2020 at 09:01, Clemens Vonrhein <[email protected]>
wrote:

> Dear Petr,
>
> On Thu, Mar 19, 2020 at 06:45:31AM +0000, Petr Kolenko wrote:
> > For those of you who are in touch with these data, would deposition
> > of unmerged intensities in P1 in the whole detector range instead of
> > complete dataset be good enough to „correctly“ re-evaluete the
> > structure? Or is there a doubt that even this approach would not
> > lead to optimal structure?
>
> It would be a step in the right direction, yes ... but:
>
>  * It assumes that all spots have been integrated and nothing else
>    than those spots: there can be cases of missed unit cell
>    duplications or incorrect enforcement of a unit cell and symmetry
>    (because those crystals always come in a known cell/SG, right?).
>
>  * We'll still be stuck with a particular intergration program and a
>    particular set of user decisions how to run it. Yes, all modern
>    data processing programs and packages are usually doing a great job
>    if run in (more or less) default mode on (more or less) good
>    crystals. But not everything is lysozyme/thaumatin/XYZ collected
>    fine-sliced on a PAD with low-dose, high-multiplicity on a well
>    calibrated instrument ;-)
>
>  * If integration was done in P1 the cell parameter restraints of the
>    (potentiually different) true SG were not enforced - which can lead
>    to incorrect cell parameters (which has knock-on effects in
>    refinement ... remember the WhatIf check for correct cell
>    parameter?).
>
>    If integration was done in a non-P1 SG and that choice was
>    incorrect: how do we know that those cell parameters didn't enforce
>    an incorrect set of cell parameter restraints, leading to poor
>    integration? Again: different programs have different ways of
>    assigning pixels (and their counts) to a reflection intensity
>    (concepts like shoebox, profile-fitting, pixel-labeling etc all
>    come to mind).
>
>  * Integration itself can be suboptimal if there are issues with the
>    crystal (ice rings, split, multiple lattices etc), the instrument
>    (damaged pixels, beam jitter, incorrect countrate cut-off handling
>    etc) or the experiment (radiation damage etc). Data processing
>    defaults might not always work correctly/best for all cases.
>
>  * The raw images allow such corrections (damaged pixels not yet in
>    pixel mask, incorrect handling of countrate_cutoff) and additional
>    analysis (e.g. radiation damage analysis a la F(early)-F(late) maps
>    [1]).
>
> So the raw integrated (not scaled/corrected) and unmerged intensities
> might indeed often be good enough, but if we are going to try and
> deposit more than just the merged and scaled intensities/amplitudes
> (as we do now) - and this will involve additional work and change from
> our side - then why not bite the bullet once and try to go all the way
> to raw images:
>
>   * The infrastructure is already in place (proteindiffraction.org,
>     data.sbgrid.org, zenodo.org, wwPDB DOIs, etc), ready for use right
>     now.
>
>   * From experience at multiple worshops: everyone is comfortable to
>     start data processing from raw images using the various software
>     tools out there that people are familiar with (while jumping in
>     half way is probably more challenging to non power-users).
>
> Anyway, just some ideas - from someone downloading nearly all deposited
> raw image data on a regular basis for testing and developing data
> processing software (and finding a lot of issues in our software this
> way ... as well as issues with experiments and sometimes the
> instrument).
>
> Cheers
>
> Clemens
>
> [1] as e.g. done in autoPROC+BUSTER
>
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