Dear Armando,
Is 1.9Å really the diffraction limit of your crystals, or do they diffract
further and is 1.9Å just a convenient resolution cutoff? In the latter case you
might be looking at truncation effects.
Best,
Herman
-Ursprüngliche Nachricht-
Von: CCP4 bulletin board [mailto:CCP4B
I am just morbidly curious what program(s) deliver/mutilate/divine these
cell constants in recent cif files:
data_r4c69sf
#
_audit.revision_id 1_0
_audit.creation_date ?
_audit.update_record 'Initial release'
#
_cell.entry_id 4c69
_cell.length_a 100.152000427
_c
Well yes, The bulk solvent model can distort the density, especially if the
ligand is large.
But it usually isnt too serious - try doing "SIMPLE" scaling and see if
that has any effect on the appearance of the density
Eleanor
On 22 July 2014 10:16, wrote:
> Dear Armando,
> Is 1.9Å really the
-BEGIN PGP SIGNED MESSAGE-
Hash: SHA1
Hi Bernhard,
A look at the methods section might give you a clue. Neither XDS nor
XSCALE create mmCIF - files (you are talking about mmCIF, not CIF -
subtle, but annoying difference), so that the choice is limited. I
guess some programmer (rather tha
I took a look at both the PDB and CIF headers for the coordinates
for 4C69 and they have normal looking numbers with three digits
following the decimal point. According to the coordinate file
header this entry was processed by PDBE. It would be interesting
to hear from the PDBE staff if the stru
Hi all,
Does anybody know of a case where the same enzyme from different species,
with reasonably invariant active site residues, perform identical
biochemical function but have significantly different substrate binding
modes/mechanism of action on the same substrate?
Thanks
Komal
Dear all,
We are planning to ligate a phospho-tyrosine containing 16aa/33aa
peptide onto a 70 kDa protein and subsequently use it for crystallography
studies. We will be using the Intein-fusion protein system (IMPACT kit from
NEB) to accomplish the ligation. The idea is to separate the
Error estimates for the unit cell dimensions in macromolecular
crystallography belong to atypical category of uncertainty estimates.
Random error contribution in most cases is below 0.001A, so it can be
neglected. Wavelength calibration error can be also made very small;
however, I do not know how
Dear Zbyszek,
when you optimise a set of parameters against a set of data, I guess you
can also provide their errors. If I understand correctly, this comes
with least-squares-routines. I only pointed out that cell errors are
listed in the XDS output (provided you refine them, of course). I am
sure
Position:
P212121 is hiring graduate students for very part time work (2-3hrs/month) to
help distribute product information.
Job Requirements:
-Know buildings on your campus other than where your lab is located
-Be based in the USA
About Us:
We distribute scientific lab supplies and chemicals. W
Doing Fluroscence scan for protein crystal at Cu wavelength prior MAD or SAD
experiment shows usually fig like this
https://www.dropbox.com/s/800463dlcmws6d4/fig.png
1- Fig A should represent X ray fluorescence scan. is it the same as X ray
absorption scan. what does count represent in fig A (i
The least-square procedure for unit cell parameter refinement provides very
precise estimates of uncertainty. Why they are so precise? Because we use many
thousands of unmerged reflections to determine the precision 1 to 6 parameters
(unit cell parameters). However, although error propagation th
Shouldn't the cell dimensions be identical in the coordinate
file and in the structure factor file? In this case they
are not.
Frances
=
Bernstein + Sons
* * Information Systems Consultants
13 matches
Mail list logo