Before deciding to change the protein sequence it is best to look at the
precipitation pattern of the protein as a function of various precipitants.
If this shows that precipitation is not within the standard range commonly
observed for other basic proteins even at high protein concentrations
then
Umar,
Check out: Czepas et al. The impact of Lys-->Arg surface mutations on
the crystallization of of the globular domain of RhoGDI, Acta D (2004)
60 275-280. They point out that sulfate ions can help mediate contacts
between arginine residues from neighboring molecules in the crystal.
Yo
dc-berlin.de/en/research/research_teams/macromolecular_structure_and_interaction/
From: CCP4 bulletin board [mailto:ccp...@jiscmail.ac.uk] On Behalf Of Jan Rash
Sent: Monday, November 02, 2009 2:40 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] Crystallization of lysine and arginine rich proteins
Following on from Stephen's comment. Jena Biosciences sell a kit that
allows you to do it quickly and easily.
check it out here:
http://www.jenabioscience.com/cms/en/1/catalog/529_jbs_methylation_kit.html
We have had success in our lab using lysine methylation to crystallise
an otherwise reca
Hi Jan,
We have tried crystallizing a similar protein without success, later on
it turned out that the protein was having a strong interaction with DNA
that was not sequence specific. You might have a case like that
Flip
Jan Rash wrote:
Dear All,
I have a question regarding the crysta
Try reductive methylation of the lysines:
Walter, T. S., Meier, C., Assenberg, R., Au, K. F., Ren, J., Verma,
A., Nettleship, J. E., Owens, R. J., Stuart, D. I. & Grimes, J. M.
(2006). Structure, 14, 1617–1622.
Cheers,
Stephen
2009/11/2 Jan Rash :
> Dear All,
>
> I have a question regarding the
Dear All,
I have a question regarding the crystallization of lysine and arginine rich
protein around 13%. So far our attempts to crystallize this protein have not
been successful although the secondary structure predictions, CD
spectroscopy measurements clearly show that this protein is folded. I
