2-DIMENSIONAL CRYSTALLIZATION OF PROTEINS ON MERCURY

被引:86
作者
YOSHIMURA, H
MATSUMOTO, M
ENDO, S
NAGAYAMA, K
机构
[1] Biometrology Laboratory, JEOL Ltd., Akishima, Tokyo
关键词
Proteins;
D O I
10.1016/0304-3991(90)90004-6
中图分类号
TH742 [显微镜];
学科分类号
摘要
A new technique to obtain two-dimensional (2D) crystals of proteins is reported. A clean surface of mercury was utilized for monolayer formation and crystallization of the protein. Two different proteins, ferritin from a horse spleen and F1-ATPase from a thermophilic bacterium (TF1), were crystallized on the clean surface of mercury in an oxygen atmosphere. Two dimensional crystals were analyzed by electron crystallography. Ferritin was found to form a hexagonal lattice with unit cell parameters a = b = 12 nm and γ = 60°. The 2D crystal of ferritin at a 2.0 nm resolution in negative stain revealed a subunit formation with P3m1 symmetry. TF1 also formed a hexagonal lattice with unit cell parameters a = b = 10 nm and γ = 60°. The reconstructed image of TF1 at a 1.8 nm resolution showed a ring structure with six peripheral constituents and minor components located in the middle hole. © 1990.
引用
收藏
页码:265 / 274
页数:10
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