Dear Saurab,
It's a shame these crystals do not diffract well - they look so good!
I assume the diffraction you saw was recorded at cryo temperatures? If so,
it is possible that you may be damaging the crystals during cryo-pretection
and cryo-cooling. Before you go too deep into changing the crystallization
conditions, I would suggest taking a shot or two at ambient temperatures
and see if the diffraction is any better. If so, you may need to optimize
the cryo protocol and not the crystallization conditions.
Regards,
Nukri

On Sun, Mar 21, 2021 at 1:04 PM Saurabh Upadhyay <saurabh807...@gmail.com>
wrote:

> Dear All,
>
> I am trying to crystalize a protein, which occurs in monomeric (60kDa) and
> tetrameric (240kDa) form. *The protein during crystallization was in
> MES buffer pH-6 *and the method of crystallization was "*Sitting drop*"
> in "*Proplex*" condition. Some of the conditions in which crystals were
> obtained are:
>
> *1) 0.1M HEPES pH-7; 10% (w/v) PEG 4000*
> *2) 0.1M Tris, pH-8; 8% (w/v) PEG 8000*
> *3) 0.1M Tris, pH-8; 25% (v/v) PEG 400*
>
> For reference, I have attached the images of the crystals observed below.
>
> *However, the diffraction pattern obtained and the resolution of crystals
> were very poor. Even some mosaicity has been observed.  *
>
> Kindly suggest some methods or modifications, to improve the resolution
> and  diffraction pattern of the crystals obtained.
>
> Thanking You,
> Sincerely,
> Saurabh Upadhyay,
> Ph.D. Scholar
> c/o Dr. Ashok kumar Patel,
> Kusuma School of Biological Sciences,
> Indian Institute of Technology, Hauz Khas,
> New Delhi-110016, India
>
>
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