>Hi
>
[quoted text clipped - 8 lines]
>2 methods ? presuming testing on a same protein. which results to
>believe ?
It's not a matter of quality or "which to believe". They measure
different things. X-ray analysis measures whatever you got into the
crystal. NMR measures whatever you measured.
Recent article -- Feb 8 issue of Nature -- on NMR with a large
protein (670 KD):
Quantitative dynamics and binding studies of the 20S proteasome by NMR
pp618 - 622
By overcoming the molecular weight limitations that have traditionally
hampered quantitative nuclear magnetic resonance spectroscopy (NMR)
studies, the dynamics of the 670-kilodalton 20S proteasome core
particle
have been explored. A selective isotope labelling scheme along with
experiments that preserve the lifetimes of the resulting NMR signals
reveal functionally important motions and interactions by recording
spectra on complexes with molecular weights up to 1 MDa.
Remco Sprangers and Lewis E. Kay
10.1038/nature05512
Abstract:
http://ealerts.nature.com/cgi-bin24/DM/y/ecQN0SpWd30HjB0BLkz0EH
+ News story
Structural biology: Molecular machinery in action p609
Nuclear magnetic resonance is the best way to study motion in
proteins, but it could be applied only to small systems. This
limitation has been overcome to reveal the dynamics of a large
protein complex.
Ad Bax and Dennis A. Torchia
10.1038/nature05566
http://ealerts.nature.com/cgi-bin24/DM/y/ecQN0SpWd30HjB0BLkr0E8
Article descriptions above are from Nature TOC.
bob