Hi,
You may also try BLEND to choose the optimal data sets before scaling
and merging
Foadi J, Aller P, Alguel Y, Cameron A, Axford D, Owen RL, Armour W,
Waterman DG, Iwata S & Evans G (2013) Clustering procedures for the
optimal selection of data sets from multiple crystals in macromolecular
crystallography. Acta Crystallogr D Biol Crystallogr 69: 1617–1632
Tassos Papageorgiou
Jarrod Mousa wrote:
Hi,
I am trying to solve the structure of a membrane protein. The protein has 12
helices and I have a good molecular replacement model that seems to work for
about half of the structure. I used chainsaw to convert the amino acid residues
to that of my protein sequence, and the density fits the structure well on one
side of the protein, but on the other side (about 5 helices), there doesn't
seem to be any density for the side chains. Has anyone had experience with
this? The completeness is high ~99% for 3.2 angstroms. The data was collected
from fairly small crystals ~ 20um.
Thanks.
