Cringe
I am spoiled.
I don’t have to collect images using film or kill whales for my haemoglobin samples.
So how do you treat the information from those that were not so lucky? I am referring to older structures that were deposited in the PDB.
For example, here is a link to the electron density server for the structure 1DCL.
The structure was solved to 2.3 A and has a Rvalue of 0.140 (wow!).
According to the EDS server the completeness is at 34.7 %. I have yet to go through the CCP4 uniqueify script and determine if the EDS calculates to 2.0 (highest resolution that the data was deposited) or 2.3 (highest resolution the data was solved), but at first glance the completeness looks to be very low.
The structure contains 9 waters which are over 70 angstroms from the protein. My guess is that these waters were incorrectly placed based on a symmetry neighbour.
The Ramachandran plot indicates nearly 11 % of the structure is comprised of outliers.
