Yuvraj

This is a tough call. may be you need to look at this database:

http://web.archive.org/web/20111011202903/http://idb.exst.jaxa.jp/db_data/protein/search-e.php

Importantly, when you click on "ex" for the tab, "cryoprotectant", a window
will pop up and you can read different kinds of cryoprotectants that have
been successfully attempted in the past. Off-course, this also depends on
type of precipitant that you used for crystallization. Apparently, this
seems as glycerol worked better in your case, may be because you have
salt-based precipitant.



Best wishes

-Z


Zaigham Mahmood Khan, PhD

Icahn School of Medicine at Mount Sinai
Department of Oncological Sciences
1470 Madison Avenue
New York

On Thu, Dec 28, 2017 at 8:28 AM, YUVARAJ I <yuvee...@gmail.com> wrote:

> Respected All,
>  I have crystallized a protein. It is forming big crystals, I have checked
> in the home source,
> Without cryoprotectant - No diffraction (blank)
> with Ethylene glycol- No diffraction (blank)
> with PEG 3350 - 7A diffraction and No ice rings
>  with Glycerol - 3.5A diffraction with ice rings
>
> I have tried soaking with glycerol different concentrations 10-30%
> glycerol from 30 secs to 5 min.
> No improvement in the diffraction quality.
>
> How to improve the diffraction quality of the crystals and avoid the big
> ice ring.
>
> I have attached the diffraction image with this mail.
>
> Thanks in advance for your valuable suggestions
>
> Regards
> Yuvaraj
>
>
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