High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy.
High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins.
Department for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Jegannath
J
Korukottu
Robert
R
Schneider
Vinesh
V
Vijayan
Adam
A
Lange
Olaf
O
Pongs
Stefan
S
Becker
Marc
M
Baldus
Markus
M
Zweckstetter
D008958:Models, Molecular; D015394:Molecular Structure; D012604:Scorpion Venoms / Q000737:chemistry*
D012604:Scorpion Venoms; C072276:kaliotoxin