I am refining a 1.3 A structure the maps look great and I notice the main chain B factors are all around 7~12. I have refined the same enzyme at resolution 2.2 A and the B factors here were around 25~30. The question that comes to mind is: Usually one will describe ordered parts of a protein vs disordered parts based on B factors. Is the higher resolution protein more ordered and that may have contributed to its stronger diffraction? Or are the B factors values artifacts of refinement? -- Yuri Pompeu
Hi Yuri,
I am refining a 1.3 A structure the maps look great and I notice the main chain B factors are all around 7~12. I have refined the same enzyme at resolution 2.2 A and the B factors here were around 25~30.
It looks all good to me.. For some statistics see page #27 here: http://www.phenix-online.org/presentations/latest/pavel_validation.pdf
Usually one will describe ordered parts of a protein vs disordered parts based on B factors.
... or occupancies (if refined or modeled alternative conformations).
Is the higher resolution protein more ordered ...
Well, I guess most of the time yes.
Or are the B factors values artifacts of refinement?
Not sure I understood this one... sorry. Good luck! Pavel.
participants (2)
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Pavel Afonine -
Yuri