Dear Vennila,

my guess is that you had a larger number of images in the batch/set starting at
180 degrees (hence the slightly incereased Rmerge for that batch) and that by
the end of that run your crystal had suffered from radiation damage (hence the
large Rmerge for the set starting at 360degrees).

You should report Rmeas instead of Rmerge and let us know about the number of
frames and the frame width in each set.

Cheers, Tim


On Sun, Jul 10, 2011 at 01:54:07PM +0100, Vennila Natesan wrote:
> Dear CCP4BB users,
> 
> In order to determine the redundancy at which the structure can be solved, I 
> divided the master
> data set of my protein into five sets with phi rotations of  45,65,90, 180 
> and 360 degrees. I got 
> the mean I/Sigma value as 22.4(11.4), 21.7(11.0), 22.7(11.2), 60.9(45.2) and 
> 15.6(8.1) respectively.
> I will be very helpful if i get any idea/possible reasons for the abnormal 
> value for 180 degree dataset.
> 
> For the information, the completeness values are 
> 75.7(78.5),92.6(92.7),99.5(97.7),99.6(97.7)and 99.5(96.4)
> respectively and values inside brackets are for highest resolution shell. 
> There was no noticable change in mosaicity
> value. The Rmerge values are 2.2,     2.4,    2.7,    3.2, and 5.7 (8.7) 
> respectively.
> 
> Thanks in advance
> 

-- 
--
Tim Gruene
Institut fuer anorganische Chemie
Tammannstr. 4
D-37077 Goettingen

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