Abstract:
:Three-dimensional crystals were obtained for the membrane domain of the human erythrocyte anion exchanger (AE1, Band 3). Protein homogeneity and stability and the delicate balance between the detergent used and the amount of phospholipids copurifying are critical to the formation of three-dimensional crystals of the AE1 membrane domain. While deglycosylation improved the protein homogeneity, its stability was significantly increased by inhibitor binding. Size-exclusion chromatography showed that the protein was monodisperse in detergents with acyl chains of 10-12 carbons over a pH range of 5.5-10.0. This pH range and the detergents that retained the protein's monodispersity were used for crystallization screening. Crystals were obtained with the protein purified in C(12)E(8), dodecylmaltoside, decylthiomaltoside, and cyclohexyl-hexylmaltoside. Five to 13 lipid molecules per protein were required for the protein crystal formation. Those crystals grown in dodecylmaltoside diffracted X-rays to 14 A. With these factors taken into consideration, ways to further improve the crystal quality are suggested.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Lemieux MJ,Reithmeier RA,Wang DNdoi
10.1016/s1047-8477(02)00010-2keywords:
subject
Has Abstractpub_date
2002-03-01 00:00:00pages
322-32issue
3eissn
1047-8477issn
1095-8657pii
S1047-8477(02)00010-2journal_volume
137pub_type
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