Herman's suggestion is very good. But I'd go one step further and try to grow 
crystals in 30-40% PEG400. Then you definitely do not need any additional 
cryoprotectant. There is a chance that your crystals are of poor quality to 
start with. In that case no cryoprotection will help. You can test that by 
collecting few diffraction images at ambient temps. If that will prove true 
that your crystals are not good enough then either that particular 
crystallization condition is not suitable for your complex or, most likely, 
more attention should be paid on getting more homogeneous protein solution.
For more project oriented advice you may contact off list.

Vaheh Oganesyan, Ph.D.
[cid:[email protected]]
R&D | Antibody Discovery and Protein Engineering
One Medimmune Way, Gaithersburg, MD 20878
T:  301-398-5851
[email protected]<mailto:[email protected]>




From: CCP4 bulletin board <[email protected]> On Behalf Of Schreuder, 
Herman /DE
Sent: Tuesday, May 18, 2021 8:33 AM
To: [email protected]
Subject: [ccp4bb] AW: [ccp4bb] sugestions on weak diffracting protein crystals

Dear Deepak,
the cryoprotection may destroy the diffraction. I would also try diffraction at 
room temperature, using special sleeves to prevent dehydration. With 20% 
PEG400, you could also try to freeze the crystals without using additional 
cryoprotectant. If you are lucky, it may work.

Best,
Herman

Von: CCP4 bulletin board <[email protected]<mailto:[email protected]>> 
Im Auftrag von Deepak Deepak
Gesendet: Dienstag, 18. Mai 2021 12:08
An: [email protected]<mailto:[email protected]>
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 oligoamide foldamer (5kDa) but these crystals diffract very poorly 
(see the diffraction pattern in picture 2).

I prepare a 1.3mM:1.3mM complex of protein: foldamer in 20mM Tris, pH 7.5 
buffer. Crystals grew in 3-5 days in sitting and hanging drop at 20 Deg C and 
25 Deg C in the following conditions:

- 20% PEG 400, 0.1M MES pH 6.0
-20% PEG 400, 0.1M Sodium Cacodylate pH 6.0

Multiple cryo used were:
-25%Glycerol in mother solution
 -30% glycerol in water
-30%PEG 400,
-35% PEG 400
-20% PEG 8000 + 40% PEG 400 mix

Kindly suggest some methods/modifications on how can I improve the resolution 
and get better-diffracting crystals. Please let me know if you need more 
information.

Kind regards,
Deepak
Ph.D. Student

PS: The protein is a DNA binding protein and I have crystallized and solved the 
structure of this protein with its DNA partner and now I crystallized it with 
our foldamers but diffraction is not good. There are multiple structures of the 
Protein+DNA complex in literature but no apo-protein structure as the protein 
needs a binding partner to crystallize. We already have solution studies 
showing a good binding.

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