I've seen flattening of the C1 atom recently in Coot - in that case the reason
was that, as the density wasn't really clear around the sugar, I'd fitted it
180 degrees rotated around the ASN-ND2---C1-NAG bond. In such cases Coot
happily flattens the sugar ring such that C1 C2 C3 C5 O5 are in a
As I see there is no chirality definition for NAG-ASN link (perhaps
there should be but then people will be unhappy even more).
Only reason i can see for this flattening is conflict between geometry
and electron density. Your example shows that even if electron density
is weak it may play a
Dear Tassos,
Am 19.04.10 17:31, schrieb Anastassis Perrakis:
snip
The sigma issue a bit more complicated.
What we call usually sigma is the root mean square deviation (rmsd) of
the map.
Lets first recall, that the variation within the protein region is
quite large, while the solvent is
Garib Murshudov wrote:
As I see there is no chirality definition for NAG-ASN link (perhaps
there should be but then people will be unhappy even more).
Only reason i can see for this flattening is conflict between geometry
and electron density. Your example shows that even if electron density
JED's example is very illustrative and it shows that chirality may
need to be added to this link definition. then sugar validation may be
easier (at least ASN-NAG with only one sugar). If chirality is wrong
then rotate around ND2-C1bond as a rigid group. Just like you do with
rotamers.
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Like so many rules of thumb, the 3-sigma fofc and 1-sigma 2fofc is a
reasonable guideline that works very well in most cases despite being
based on a flawed assumption. The 0.3% chance of a peak being above 3
sigmas assumes that the histogram of electron density values is
Gaussian. It is
Hello all
I apolozize for a off topic question on BB.
I am working with small proetin-protein complex, each have molecular weight
10kDa. I elute this N-terminal His-tagged complex through Ni-NTA resin in
50mM of NaH2Po4, 0.3M of NaCl, 5% glycerol and 250mM of Imidazole.Similarly,
Lysis buffer
Hello BB
I apolozize an off topic query.
I am working with small proetin-protein complex of 24kDa. I purify this
N-terminal His-tagged complex through tylon resin in 20mM of Tris pH-8.0,
0.3M NaCl . After purification this protein complex are dialysed in 20mM
tris pH=8.0.I am able to purify
Hi Peter,
we had a four similar cases recently. What really helped us was to add urea in
amounts of 1-2 M. We tested the possible influence on secondary structure by
limited proteolysis and CD/Trp-fluorescence and it seemed the protein
maintained the same overall conformation as in the absence
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