MBB 222 Lecture Notes - Lecture 12: Nuclear Magnetic Resonance Spectroscopy, X-Ray Crystallography, Super-Resolution Imaging

• School: Simon Fraser University
• Department: Molec Biol & Biochem
• Course: MBB 222
• Professor: Irina Kovalyova

Document Summary

Techniques that are useful for imaging and structural analysis of different objects. You cannot image things much smaller than the wavelength of light you are using. (an exception is super-resolution microscopy, a nobel prize-winning technique). Methods of protein structural analysis: nuclear magnetic resonance spectroscopy (nmr), x-ray crystallography, electron microscopy (em) The quality of a protein structure depends i(cid:374) part o(cid:374) the (cid:862)resolutio(cid:374)(cid:863) of the structure: the minimum distance that two objects can be apart and still be seen as two separate objects. The smaller this distance is, the higher the resolution of the structure. Note: a (cid:862)high resolutio(cid:374)(cid:863) em reconstruction (e. g. , 5 ) would be co(cid:374)sidered a (cid:448)ery (cid:862)lo(cid:449) resolutio(cid:374)(cid:863) structure in the context of nmr or x-ray crystallography. In x-ray crystallography (cid:862)high resolutio(cid:374)(cid:863) means atomic resolution, ~1 , where individual atoms can be resolved. The deter(cid:373)i(cid:374)atio(cid:374) of a protei(cid:374)"s stru(cid:272)ture (cid:271)y x-ray crystallography involves several steps. A beam of ray is directed at a protein crystal.