Electron and atomic force microscopy of membrane proteins

被引：32
|
作者：
Heymann, JB [1 ]
Muller, DJ [1 ]
Mitsuoka, K [1 ]
Engel, A [1 ]
机构：
[1] KYOTO UNIV, FAC SCI, DEPT BIOPHYS, KYOTO 60601, JAPAN
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 1997年 / 7卷 / 04期
关键词：
D O I：
10.1016/S0959-440X(97)80120-0
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Electron crystallography is becoming a powerful tool for the resolution of membrane protein structures. The past year has seen the production of a bacteriorhodopsin model at 3.5 Angstrom and the structure of aquaporin 1 approaching atomic resolution. Determination of surface topographies of 2D crystals using the atomic force microscope is similarly advancing to a level that reveals submolecular details. As the latter is operated in solution, membrane proteins can be observed at work.
引用
收藏
页码：543 / 549
页数：7
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