Hi Deepak
In my opinion, rMMS microseeding, ie adding crushed seed crystals into *random
screens*, should be used routinely in most crystallization projects. It
gives much more control, in particular you can control the number of
crystals per drop.
In a case like this, I would use it straight aw
Hi Deepak,
If this is a metalloprotein, include higher concentration of the metal in
the crystallization drop. It may act as a glue in the interfaces and give
you a good crystal.
Jackie Vitali
Cleveland State University
On Tue, May 18, 2021 at 6:20 AM Deepak Deepak
wrote:
> Dear all,
>
> I ha
If the foldamer(s) have exposed flexible parts they may impede ordered
crystallisation. Perhaps some minor tweaks to the foldamer or foldamers you are
co-crystallising with might lead to a better crystal contacts?
For example removing one or a few residues from the end(s) or shortening a loop.
M
edical Research Institute
700 Ellicott Street | Buffalo, NY 14203-1102
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From: CCP4 bulletin board On Behalf Of Deepak Deepak
Sent: Tuesday, May 18, 2021 6:08 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] sugest
...@medimmune.com>
From: CCP4 bulletin board On Behalf Of Schreuder,
Herman /DE
Sent: Tuesday, May 18, 2021 8:33 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] AW: [ccp4bb] sugestions on weak diffracting protein crystals
Dear Deepak,
the cryoprotection may destroy the diffraction. I would
,
Herman
Von: CCP4 bulletin board Im Auftrag von Deepak Deepak
Gesendet: Dienstag, 18. Mai 2021 12:08
An: CCP4BB@JISCMAIL.AC.UK
Betreff: [ccp4bb] sugestions on weak diffracting protein crystals
Dear all,
I have got multiple crystals (see picture 1) of a protein (8kDa) with a helical
aromatic
Dear Deepak,
I have a few suggestions:
1) First you can send it to synchrotrons, particularly microfocus beamlines
and shoot as many good in-house diffracting crystals.
2) Setting up crystallisation by micro batch method under Al's oil at
various vapour exchange rate may help. But
