nternal 432092)
> Section Editor Acta Crystallographica F
> https://journals.iucr.org/f/
>
> On 4 Feb 2023, at 15:48, kavyashreem wrote:
>
> Dear all,
>
> Sorry for the confusion created, I did not mean that a protein would have fit
> in the small unit cell. My ques
seems like a dirty trick, if your
> expectation is that only protein crystals can do that. The brightfield white
> light image of the crystals is also consistent with not-protein crystals,
> because of the high refractive index contrast between the crystals and the
> mother liquor.
>
&
of Biochemistry
> https://www.biochem.uni-luebeck.de [6]
> phone: +49-451-3101-3105
> Ratzeburger Allee 160
> 23562 Lübeck
> Germany
> --
>
>> Am 03.02.2023 um 09:22 schrieb kavyashreem :
>>
>> Dear all,
>>
>> We crystallized a protein (30kDa) + liga
ethods. You never know, it
> could be something interesting.
>
> Mark J van Raaij
> Dpto de Estructura de Macromoleculas, lab 20B
> Centro Nacional de Biotecnologia - CSIC
> calle Darwin 3
> E-28049 Madrid, Spain
> tel. +34 91 585 4616 (internal 432092)
> Sectio
on Editor Acta Crystallographica F
> https://journals.iucr.org/f/
> https://namedrop.io/markvanraaij
>
>> On 3 Feb 2023, at 09:22, kavyashreem wrote:
>>
>> Dear all,
>>
>> We crystallized a protein (30kDa) + ligand (by cocrystallization), in the
>> condition
gt;
> I am pretty sure you crystallised the ligand, or TCEP actually.
>
> Also, if you look at the diffractions pattern, its clear the crystal
> diffracts beyond 1.0A, diffraction spots are really very very very strong at
> 2.0A.
>
>> On 3 Feb 2023, at 09:22, kavyas
tallographica F
> https://journals.iucr.org/f/
>
> On 4 Feb 2023, at 15:48, kavyashreem wrote:
>
> Dear all,
>
> Sorry for the confusion created, I did not mean that a protein would have fit
> in the small unit cell. My question was -
>
> 1. Why are there close
91 585 4616 (internal 432092)
> Section Editor Acta Crystallographica F
> https://journals.iucr.org/f/
>
> On 4 Feb 2023, at 15:48, kavyashreem wrote:
>
> Dear all,
>
> Sorry for the confusion created, I did not mean that a protein would have fit
> in the small uni
Dear All,
Has anyone worked on a protein which is highly soluble even at 80mg/ml?
We have one such candidate, which does not precipitate even at 80mg/ml
instead forms phase separated globules in crystallization plate, which
eventually hardens over a period of 1 to 1.5 months (which is
f
>
> 2. Many years ago, we did some data mining of the crystallization conditions
> in a remark in the PDB. The concentrations that people reported are below.
> There were eight reports where over 100 mg/mL was used. It only goes up to
> 2004.
>
>> https://www.douglas.co.uk/PDB_data.ht
concentrations (will try)
10. Organic solvents (though about it)
11. Mutations (ongoing)
Thank you
Regards
Kavya
On 2024-02-05 15:57, kavyashreem wrote:
> Dear All,
>
> Has anyone worked on a protein which is highly soluble even at 80mg/ml?
>
> We have one such candid
p alter the protein properties and facilitate new crystal
> contacts. Additionally, it may be worth experimenting with reduced salt
> concentrations or using a salt-free buffer, akin to using water in place of a
> buffer.
>
> PMID: 32541044
> PMID: 26850170
>
> W
; to electrostatic repulsion?
>
> Hi Kavyashreem
>
> The project that I mentioned, where we looked at the crystallization
> conditions reported in the PDB, also looked at the areas of amino acids (and
> atoms) on the surfaces of proteins and tried to correlate the various group
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