Dear Colleague,
This year the Synchrotron Radiation (SR) User Meeting
http://www.diamond.ac.uk/ForUsers/SRUser07/default.htm will be held
from Thursday 13th to Friday 14th September 2007 at Diamond Light
Source, Oxfordshire. The objectives of this meeting are to bring
together the entire United
Well - this (expert??) would suggest using SCALE SIMPLE -
SCBULK is a fudge which has some theoretical justification if you have
measured very complete and accurate low resolution data, but seeing most
people havent done this it remains a fudge factor
The justification is related to average
Dear colleagues,
here some comments about our Hg ripple problem - many thanks to all your
answers:
Indeed we were not able to completely get rid of the ripples (as stated
by Bart Hazes: not really affecting the biological conclusions - but
anyway!). Summarizing the suggested problems are:
Jie Liu wrote:
Dear CCP4ers:
Does anyone know an existing program to calculate the lateral
displacement---the vertical offset, measured as a fraction of the
the heptad repeat---of neighboring helices in coiled coils or helix
bundles, either parallel or antiparallel?
Your input is greatly
Dear All:
This is off topic but I would rather try here first.
I am wondering whether Dnase could be a contaminant during the nickel
affinity purification of a his.tag protein expressed using pET29b. The
cells were disrupted using sonication only. Very high yield (30 mg/liter
of cell culture).
Dear All,
It will be a great help for us if some users can
suggest about Bruker Microstar-H with Helios optics
and MarDTB image plate. Please tell the performance
about this if some one has this combination. How
difficult is to change the filament and after how many
hours. Is there any problem in
Since Jie Liu is talking about coiled coils and heptad
repeat, I think what may be needed is the displacement
along the bundle axis. So an expression for the best
bundle axis line, and then the projection of different
C-a's onto that line to measure the difference between
them?
Ed
Eleanor Dodson
Dear Ed, Eleanor, Pratap and CCP4ers
Thank you all for the replies.
In Jane S. Richardson's Alacoil paper (Protein Science,
1995, 4:2252-2260), they defined the vertical offset
as follows: choosing the Ca of the a heptad position
on one helix as the reference zero level and position
a+7 as level
Hi,
This is an intriguing question :) It's quite hard to test for 'stray'
nucleases when you potentially have mg/ml amounts of 'real' nuclease.
Typically, the DNAse contamination of proteins purified from E. coli is
not massive - especially after several purification steps. Otherwise, the
Dear CCP4ers,
My turn to ask an unrelated question :) Sorry!
Does anyone here have an EndNote style for the Journal of Structural
Biology? I am a lazy slob, and would like to check before making my own.
The EndNote online collection does not seem to have one. Alternatively, if
you can suggest an
Dear Narayanan,
you could simply test that by a negative control: transform your cells with
an empty vector, and follow the same (exact) purification protocol. No DNase
activity there = probably no DNase contaminant in your original prep.
Cheers
Filip
On 8/6/07, Narayanan Ramasubbu [EMAIL
Hi,
I am trying to make figures using the Windows version of povscript. However,
it doesn't seem to recognize the slab command.
The error message is: Error: syntax error: line number ? in file ?, at
slab.
If I skip the slab line and let the software automatically calculate a slab
number, it
hi all,
I am working on a protein for which we get nicely diffracting
crystals but the problem is that the crystals grow from anywhere between
4-6 months. Does anyone has any general suggestions as to what things
can be changed or tried to speed up the process. Any help or suggestions
Hi,
Temperature is one obvious factor that comes to mind.
If you have access to MS, you could check the protein from the
crystallization drops - find out if there's something 'chemical' going on
such as proteolysis, modification of some sort, etc. - this has happened
to me once before, the
On Mon, 2007-08-06 at 15:50 -0400, Neeraj wrote:
hi all,
I am working on a protein for which we get nicely diffracting
crystals but the problem is that the crystals grow from anywhere between
4-6 months. Does anyone has any general suggestions as to what things
can be changed or
Thank you all who sent in the link to the correct endnote library -
somehow I failed to find it on the endnote website, which proves that not
only I am a lazy slob, but a blind one as well :)
Thank you,
Artem
Hi Neeraj,
There are several ways to approach this problem. Of course, this also
depends on your sample and the amount you have available.
1. Probably the first thing to try is seeding (streak or micro).
2. You could try with higher protein and/or precipitant concentration.
3. If you have enough
Hello everyone,
Thank everybody for the good suggestions.
Especially I thank Prof. Eleanor Dodson for her many times' help.
Finally, I found that there is an ice ring in the data as the suggestion of
Prof. Eleanor Dodson.
After I cut out ice rings, Rfact and Rfree are 0.175 and
Hi Neeraj,
Two more tricks:
1. Open the cover slip a bit to allow for faster evaporation. It
worked well on one of my proteins.
2. in-situ proteolysis: Acta Crystallograph Sect F Struct Biol Cryst
Commun. 2006 Oct 1;62(Pt 10):1041-5.
Good luck.
Zhen
Quoting Neeraj [EMAIL PROTECTED]:
hi all,
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