Hi,
You could try XDS and input your unit cell from one crystal, then decide
whether you're happy with the outcome for the other crystal.
Boaz
Boaz Shaanan, Ph.D.
Dept. of Life Sciences
Ben-Gurion University of the Negev
Beer-Sheva 84105
Israel
Phone: 972-8-647-2220 Skype:
A postdoctoral position is available immediately at the University of
Massachusetts Medical School in the Korostelev Lab
(http://www.umassmed.edu/bmp/faculty/korostelev.cfm).
The focus of research in the lab is on translation and translation regulation.
We use X-ray crystallography to study
A Research Technician position is available at the High Throughput
Crystallisation laboratory of the EMBL Grenoble Outstation.
You will find the details in the link below.
https://intranet.embl.de/hr/jobs/searchjobs/index.php?newlang=1newms=srsearchregion=670
Dear All,
A Research Technician position is available at the High Throughput
Crystallisation laboratory of the EMBL Grenoble Outstation.
You will find the details in the link below.
http://www.embl.de/aboutus/jobs/searchjobs/index.php?newlang=1newms=srsearchregion=670
On 17/05/11 15:35, Afshan Begum wrote:
Dear All,
I would like to introduce carbamylated lysine in a structure because i
have used beta-mercaptoethanol in a protein solution and lysine was
carbamylated with this but i faced a problem to introduce this residue
in my structures i have not find
Dear Pascal and Matthias,
I am sorry for the delay of reply, thanks very much for your suggestions on the
glycosylation protein. Now I am trying to do a stable cell line with CHO lec
3.8.2.1 cells, this cell line could express protein with shorter glycans. I
hope several weeks later I could
I have limited cautionary experiences with Lec1 CHO expression, although with a
highly and complex glycosilated protein. Subsequent glycan analysis showed that
the glycans are indeed more homogeneous and less branched, but not exclusively
the Man5GlcNac2 type that are reported/expected. There
The HEK293S/ I-/- strain (Reeves et al PNAS 2002) does not lack glycosylation
capacity. It is deficient in a key glucosyl transferase responsible for adding
glycans beyond the Man5GlcNac2. This produces N-linked glycosylated proteins
with homogeneous glycan trees.
We recently established
Hi,
I have a diffraction data-set from a hexagonal rod shaped crystal, to about 2.0
Å. The problem comes when I try to process the data - Mosflm won't index it,
and XDS indexes it as P622, but the unit cell is too small to contain even a
single molecule of my protein. I have tried
In general, the Rmerge and Rmeas should get better with a lower symmetry
spacegroup, so that's weird.
Maybe you didn't crystallize what you thought you crystallized. Do people
runs gels anymore on crystals to get an idea of what's in the crystal or do
they do MassSpec?
I think another way to go
Dear Wei,
If I understood correctly your description, the protein aggregates when
produced whith complex N-linked glycosylation, and behaves better when the
glycosylation is immature (i.e. following kifunensine treatment I suppose ?).
May I suggest that this is a rather atypical situation?
It
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