ight source and better optics.
> >>
> >> Thanks,
> >> Clint
> >>
> >>
> >> Clint Spiegel
> >> Assistant Professor, Chemistry
> >> Western Washington University
> >> 516 High Street
> >> Bellingham, WA 98225-9150.
--
+-+-+
| Dr. Jens T. Kaiser | Office: +1(626)395-2662 |
| California Institute of Technology | Lab:+1(626)395-8392 |
| m/c 114-96 | Cell: +1(626)379-1650 |
| Pasadena, CA 91125, USA | Email: kai...@caltech.edu |
+-+-+
MAIN does that for ages (n_molecules->generate_others). Also, the new COOT can
do that (look in the - rather cluttered - treasure
chest 'Extensions'->'NCS'->'Copy NCS chain')
HTH
-j.
On Wednesday 26 November 2008 00:25:12 Prakash Rucktooa wrote:
> Dear Olga,
>
> I have also encountered the sam
I switched to mineral oil (same as for pcr). You can apply it either with a
1mL pipet tip or with use a glass vial with the same diameter as the linbro
wells as a stamp. This is much nicer as round cover slips do self-center and
opening is gentler on the slips, too.
HTH,
Jens
On Thursday 27 N
But there is a more fundamental difference. Crystallography determines the
positions (more or less accurate) whereas NMR measures distances between
certain atoms. NMR is local, 1-dimensinal information that -with enough data-
can be used to generate a three dimensional model compatible with it,
I have found the people at the pdb very helpfull and accomodating.
I think the key point is to /discuss/ the issue with them instead
of 'demanding' a certain way of deposition. The depositors may have their
reasons for certain namings, but the pdb has its reasons too, often based on
a much broad
I usually do that with a simple selection. it works in MAIN, CNS, RASMOL
below syntax for RASMOL (because it comes w/ ccp4) assuming they are
superimpsosed, waters have chain names W and X, respectivly, and your cutoff
for conservedness(?) is 0.7A:
select (water and *:W) and within(0.7,(wat
Dear Filip and others,
To play Devils advocate, this could also (in the absence of strongly
supportive biochemical data) be interpreted as a crystal artifact, with the
weakly binding ligand not forming a physiologically relevant contact but
merely occupying the - haphazardly - empty space in t
You have to sort the mosflm files together. i.e in
ccp4i>datareduction>sort/modify/combine you add both mtz files (with help of
[add file] button. then you scale them in two runs in scala (run 1 1 to 36 run 2
38 to 180, in case that's not obvious).
ccp4 uses (unfortunately) 'merging' in several
Hi Anita,
what I do in pathological cases is
synchrotron
postref beam 0 usebeam off
I think usebeam off is not necessary. Like that the mosaicity is not refined at
all. I think that's the only way.
cheers,
jens
Anita Bentley wrote:
Dear MOSFLM specialists,
I am trying to treat rather diff
Sarathy (and Todd)
DMF is usually used for dimethyl formamide. From the name I have no idea what
"dimethyl fluoride" may be (methylene difluoride, though wrong, is used for
difluor methane,but that's not mixable with water, and only a liquid at low
temperature ;-) )
Todd,
If your protein has
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