Hi Alexandre,

I was curious if I could also get a copy of the illustrations if it wont be
too much trouble?  I was more curious about 0.0 - 4.0 Ang region if that
saves you some effort.

Thank you for this.

Matthew Merski

On Tue, Nov 28, 2017 at 4:12 PM, Alexandre Ourjoumtsev <
alexander.ourjoumt...@univ-lorraine.fr> wrote:

> Dear Vincent,
>
> first, certainly, you can continue to a higher resolutions distinguishing
> further details :
>
> 3.3 A - nucleic acid pairs
> ....
> 1.2 A - atomic details
> 0.9 A - deformation density
> (by the way, there was a relevant work, I think, by E.Blanc and G.Bricogne
> beginning of 2000, about some crucial high-resolution cut-offs).
>
> Second, a convenient scale for this detail analysis is logarithmic (we
> discussed this a few years ago in Acta Crsyt D); the limits you are talking
> about become more or less uniform in this scale.
>
> Third, at low resolution the situation is not at all so simple as you
> wrote. For example, images at 10-12 A may show neither "more ordered
> envelopes" nor "secondary structure elements" but only a "big mess". This
> is really the "worse resolution" to work with. I can send / give you
> off-list some illustrations.
>
> Best regards,
>
> Sacha Urzhumtsev
>
> ----- Le 28 Nov 17, à 15:44, vincent Chaptal <vincent.chap...@ibcp.fr> a
> écrit :
>
> Hi,
>
> I've been searching but can't find what I am looking for so I thought I
> ask specialists.
>
> I am curious about the link between resolution limits of reflections on
> the detector, and what features are ordered in real space.
> I saw the great movie by James Holton on resolution and features in the
> electron density map, but I am looking for something more general.
> I am thinking that a reflection on the detector originates from something
> ordered within the crystal. The level of order would be different at
> different resolution.
>
> If you can help me fill the void in this phrase:
> I see spots at __A resolution, therefore I know that _____ features are
> ordered in my crystal.
>
> intuitively, I would build the following scale:
> 20A : the envelope is ordered
> 10A: a finer envelope is ordered
> 6A: alpha helices are ordered
> 4-5A: beta sheets are ordered and some residues
> 3-4A: residues start to be ordered
> >3A: more and more order.
>
> Has this been described somewhere? I would appreciate any comments and
> reevaluation of this scale.
>
> Thank you in advance.
> All the best
> Vincent
>
>
> --
>
> Vincent Chaptal, PhD
>
> Institut de Biologie et Chimie des Protéines
>
> Drug Resistance and Membrane Proteins Laboratory
>
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