Hi, A quick search of the CCP4BB archive reveals a couple of previous conversations on this topic. I’ll link them here to save repetition — reading through should give you a pretty good idea:
https://www.mail-archive.com/ccp4bb@jiscmail.ac.uk/msg42526.html https://www.mail-archive.com/ccp4bb@jiscmail.ac.uk/msg30339.html I (personally) think the best answer from these was to look at the TLS-subtracted residuals (ie. total B-factor - TLS component) — can’t remember who sent it, off the top of my head. (Of course, looking at the change in the TLS components is also interesting, as Ethan Merritt points out in one of the replies.) Nick Nicholas Pearce, PhD, Post-doctoral Researcher, University of Utrecht On 9 Aug 2018, at 11:54, Santhosh Gatreddy <santhoshgl2...@gmail.com<mailto:santhoshgl2...@gmail.com>> wrote: Hi all, I have to compare the B-factors of three of my ligand bound structures of the same protein which were diffracted to 1.85, 1.98 and 2.01 A resolution. Is it necessary to normalize the B-factors of these structures (dimer in ASU) before comparing them to understand the ligand induced stability. Thanks for Your suggestions, Santhosh ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1 ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/webadmin?SUBED1=CCP4BB&A=1
