Protein-detergent interactions in single crystals of membrane proteins studied by neutron crystallography

Conference · Sat Dec 31 00:00:00 EST 1994

DOI:https://doi.org/10.1007/978-1-4615-5847-7_23· OSTI ID:381089

Timmins, P A ^[1]; Pebay-Peyroula, E ^[2]

---

1. ILL, Grenoble (France)
2. 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. (LANL), Los Alamos, NM (United States)
• OSTI ID: 381089
• Report Number(s): LA-UR-96-634; CONF-9410223-; ON: DE96006681; TRN: 96:005198-0022
• Resource Relation: Conference: 3. conference on neutrons in biology, Santa Fe, NM (United States), 24-28 Oct 1994; Other Information: PBD: [1994]; Related Information: Is Part Of Proceedings of the neutrons in biology conference, Santa Fe, NM, October 1994; Schoenborn, B.P.; PB: 354 p.
• Country of Publication: United States
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
66 PHYSICS
PORINS
NEUTRON DIFFRACTION
MOLECULAR STRUCTURE
CRYSTALLOGRAPHY
MEMBRANE PROTEINS
PROTEIN STRUCTURE
SCATTERING
HEAVY WATER
CONTRAST MEDIA