Crystallization in cubo: general applicability to membrane proteins.
Obtaining well ordered crystals of membrane proteins is the single most serious stumbling block in the pursuit of their high-resolution structures. The applicability of lipidic cubic phase-mediated crystallization is demonstrated on a diverse set of bacterial membrane proteins: two photosynthetic reaction centres, a light-harvesting complex and two retinal proteins, halorhodopsin and bacteriorhodopsin. Despite marked differences in molecular dimensions, subunit composition and membrane origin, one single lipid, monoolein, is sufficient to form a crystallization matrix for all the aforementioned systems. Therefore, the lipidic cubic phase approach is proposed as a general method for crystallizing membrane proteins.
Chiu
M L
ML
Department of Molecular Microbiology, Biozentrum, University of Basel, Switzerland.
Nollert
P
P
Loewen
M C
MC
Belrhali
H
H
Pebay-Peyroula
E
E
Rosenbusch
J P
JP
Landau
E M
EM
D001426:Bacterial Proteins / Q000737:chemistry*; D001436:Bacteriorhodopsins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D019617:Halobacterium salinarum; D025602:Halorhodopsins; D008565:Membrane Proteins / Q000737:chemistry*; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry; D012242:Rhodobacter sphaeroides; D012241:Rhodopseudomonas
D001426:Bacterial Proteins; D025602:Halorhodopsins; D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D001436:Bacteriorhodopsins