Structure determination of aligned systems by solid-state NMR magic angle spinning methods.
Single crystal rotational echo double resonance (REDOR) experiments can be used to determine the three-dimensional orientation of heteronuclear bond vectors in an amino acid, as well as the crystal's orientation relative to the rotor fixed frame (RFF). We also demonstrate that for samples uniaxially aligned along the rotor axis, the polar tilt angle of a bond vector relative to the RFF can be measured by use of an analytical expression that describes the REDOR curve for that system. These bond orientations were verified by X-ray indexing of the single crystal sample, and were shown to be as accurate as +/- 1 degrees .
Gross
Benjamin J
BJ
Department of Chemistry, Columbia University, 3000 Broadway, New York, NY 10027, USA. bjg30@columbia.edu
Tanski
Joseph M
JM
McDermott
Ann E
AE
D000409:Alanine / Q000032:analysis* / Q000737:chemistry*; D000465:Algorithms; D016880:Anisotropy; D003198:Computer Simulation; D003461:Crystallography / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D044367:Phase Transition; D011208:Powders / Q000032:analysis / Q000737:chemistry; D012399:Rotation; D013113:Spin Labels
D011208:Powders; D013113:Spin Labels; D000409:Alanine