A lipidic-sponge phase screen for membrane protein crystallization.
Structure
; 16(7): 1003-9, 2008 Jul.
Article
en En
| MEDLINE
| ID: mdl-18611373
ABSTRACT
A major current deficit in structural biology is the lack of high-resolution structures of eukaryotic membrane proteins, many of which are key drug targets for the treatment of disease. Numerous eukaryotic membrane proteins require specific lipids for their stability and activity, and efforts to crystallize and solve the structures of membrane proteins that do not address the issue of lipids frequently end in failure rather than success. To help address this problem, we have developed a sparse matrix crystallization screen consisting of 48 lipidic-sponge phase conditions. Sponge phases form liquid lipid bilayer environments which are suitable for conventional hanging- and sitting-drop crystallization experiments. Using the sponge phase screen, we obtained crystals of several different membrane proteins from bacterial and eukaryotic sources. We also demonstrate how the screen may be manipulated by incorporating specific lipids such as cholesterol; this modification led to crystals being recovered from a bacterial photosynthetic core complex.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Cristalización
/
Membrana Dobles de Lípidos
/
Proteínas de la Membrana
Idioma:
En
Revista:
Structure
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
/
BIOTECNOLOGIA
Año:
2008
Tipo del documento:
Article
País de afiliación:
Suecia