Well, there is an obvious relation between cell dimensions - what is the
translation vector you find at 41%
You say the native structure has 3 monomers - I would send those
coordinates to the PISA application at the EBI, and see what the interfaces
are and make sure you are using closely packed search models - eg you may
find there is a closely packed trimer which is built using symmetry
equivalent molecules to your native solution..
Hard to answer without more information though.
ie space group, relative size od protein and complex etc..
Eleanor
On Feb 27 2012, intekhab alam wrote:
Hi all
I have collected 2 datasets; one for the native proteins (2.3Å resolution)
while other is for a protein-protein complex (3.5Å resolution). The unit
cell parameters for the native are a=120, b=196, c=109, a=g=90, b=114,
while for the complex data it is a=122, b=197, c=300, a=g=90, b=93. I have
successfully got a MR solution and refined the native dataset with 3
monomers in the asymmetric unit. Analysis of the protein complex dataset
shows 41% pseudo translation and so far there is no success in molecular
replacement for this dataset. Can anyone please suggest me ways to solve
this problem. i already have tried different templates like monomer, dimer,
trimer, tetramer etc with truncations of loop region. i am using phaser as
well as molrep programs.
Regards
--
Professor Eleanor Dodson
YSNL, Dept of Chemistry
University of York
Heslington YO10 5YW
tel: 00 44 1904 328259
Fax: 00 44 1904 328266
