Another factor may be that phenix.refine does not make a full use of
experimental phase information in its calculation of the error
parameters - I've been discussing this with Peter, Randy and Ralph. I
don't know that this is the cause, but I see inferior results when
recycling buccaneer with
phenix.refine also might not (by default) use missing data in map calculation.
AFAIK, refmac fills in missing data with DFc. Phenix doesn't (maybe
this changed now).
When your high resolution shells are incomplete (like when using the
anisotropy server to perform elliptical data truncation, or etc
Can one make it? If so, what's the keyword? Because I couldn't it in
the online docs.
Cheers
phx
Peter Zwart wrote:
phenix.refine also might not (by default) use missing data in map calculation.
AFAIK, refmac fills in missing data with DFc. Phenix doesn't (maybe
this changed now).
When your h
Dear all
A new version of the automatic molecular replacement webserver is now
available. Major new option is the link with the automatic molecular
replacement system - arp/warp.
If automatic molecular replacement is successful then balbes can send
the results to arp/warp server for model b
Dear Neeraj --
On 26 Sep 2008, at 22:48, Neeraj wrote:
Is there an easy way to do this in pymol which will help me rotate
only a small fragment of the protein while keeping everything else
static.
What you can do is to generate two coordinate files, one without your
loop, one with, and mo
