(A tad delayed)
Actually, typically we set up crystal trials for both cleaved and
uncleaved protein right away at the same time (if there's enough protein
and the cleavage works).
Cheers
phx
On 07/01/2011 15:10, Bosch, Juergen wrote:
I vaguely remember a paper by Aled Edwards, where they did the
statistics for their targets at SGC. As far as I recall they engineer
with cleavable tag purify and cyrstallize it first with tag and only
if they don't get crystals or a structure they cleave off the tag and
rerun the screens. I think the numbers where 30% of the proteins have
been cleaved.
Jürgen
-
Jürgen Bosch
Johns Hopkins Bloomberg School of Public Health
Department of Biochemistry & Molecular Biology
Johns Hopkins Malaria Research Institute
615 North Wolfe Street, W8708
Baltimore, MD 21205
Phone: +1-410-614-4742
Lab: +1-410-614-4894
Fax: +1-410-955-3655
http://web.mac.com/bosch_lab/ <http://web.me.com/bosch_lab/>
On Jan 7, 2011, at 9:40 AM, Snijder, Arjan wrote:
Dear all,
Best wishes for the new year!
I am looking for some statistics about the fraction of protein
structures in the pdb that are actually crystallized with a His tag,
and from those crystallized with a His tag whether these construct
were engineered with a cleavable tag or not. Has anybody done such an
analysis and would want to share the outcome?
In the mean time I will mentally prepare myself for re-freshing my
perl knowledge to write a script to do such an analysis. Any
suggestions on how to quickly analyse this would be appreciated.
cheers
Arjan
*Arjan (Harm Jan) Snijder*
Associate Principal Scientist
Astra Zeneca R&D, Mölndal
Discovery Enabling Sciences and Capabilities, DECS
SE-431 83 Mölndal Sweden
tel: ++46 31 7763691
arjan.snij...@astrazeneca.com <mailto:arjan.snij...@astrazeneca.com>
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