Protein-detergent interactions in single crystals of membrane proteins studied by neutron crystallography
- ILL, Grenoble (France)
- IBS-UJF Grenoble (France)
The detergent micelles surrounding membrane protein molecules in single crystals can be investigated using neutron crystallography combined with H{sub 2}O/D{sub 2}O contrast variation. If the protein structure is known then the contrast variation method allows phases to be determined at a contrast where the detergent dominates the scattering. The application of various constraints allows the resulting scattering length density map to be realistically modeled. The method has been applied to two different forms of the membrane protein porin. In one case both hydrogenated and partially deuterated protein were used, allowing the head group and tail to be distinguished.
- Research Organization:
- Los Alamos National Lab., NM (United States)
- OSTI ID:
- 381089
- Report Number(s):
- LA-UR--96-634; CONF-9410223--; ON: DE96006681
- Country of Publication:
- United States
- Language:
- English
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