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There seem to be systematic absences along l.
Checking how those get indexed should tell you if the beam center
is off, and if so by how much to correct it.

Mounting in capillaries can be pretty brutal to crystals,
especially if you are out of practice.
Try Bob Thorne's system instead- loop the crystal as usual but
instead of freezing it slip the pin into one of his polymer tubes
with a bit of mother liquor in the end. Get the beamline people to
bring out the old FTS temperature controller and set it for
2 degrees C, and you're all set!

http://www.mitegen.com/products/micrort/micrort.shtml


Dear all,
hopefully some of you may be able to make a few suggestions for a project I'm 
currently working on. It's a protein complex which crystallises to produce 
small crystals (max. dimension 0.1 mm, with rod morphology).
It doesn't diffract in-house but does at synchrotron sources. The data is very 
anisotropic and a massive unit cell. I believe the indexing is P6 or P622 with 
cell dimensions 87.8, 87.8, 629.5.
I've had a lot of problems scaling any data (I think, mainly due to overlaps or 
poor data and the anisotropy of diffraction). The crystals are frozen (but I do 
intend on trying some capillary mounted samples). Any suggestions regarding 
processing the data or optimising the data collection strategy would be 
wellcomed.

If you would like to look at a typical frame collected at the ESRF on id23 at a 
distance of 445mm and a wavelength of 1.0 Ang. please feel free to download it 
from here:

http://www.nottingham.ac.uk/~pazxtal

Regards,
Paul..

##################################
Dr Paul A. McEwan
Post-Doctoral Research Fellow
Protein Crystallography Group
Centre for Biomolecular Science
Clifton Boulevard
University of Nottingham
Nottingham
NG7 2RD
Tel: 0115 8468009
http://www.nottingham.ac.uk/~pazxtal
##################################


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