An atomic force microscopy investigation of protein crystal surface topography

被引：8

作者：

Levadoux M. ^{[1
]}

Gadea J. ^{[1
]}

Flandrin P. ^{[1
]}

Carlos E. ^{[1
]}

Aswad R. ^{[1
]}

Panuel M. ^{[1
]}

机构：

[1] Department of Orthopedic Surgery, French Naval Hospital St Anne, Toulon

来源：

European Biophysics Journal | 2001年 / 30卷 / 5期

关键词：

Atomic force microscopy; Crystal growth; Ferritin; Lysozyme; Protein crystals;

D O I：

10.1007/s002490100165

中图分类号：

学科分类号：

摘要：

Tapping mode atomic force microscopy was employed to study the surface structure of different protein crystals in a liquid environment. The (101) face of hen egg-white lysozyme crystals and the (111) face of horse spleen ferritin crystals were studied. On the (101) face of lysozyme crystals we observed islands delimitated by micro-steps and elongated in the [010] direction. The elongation direction coincides with the preferential growth direction predicted by a growth model reported in the literature. The islands observed on the ferritin (111) face are also delimitated by micro-steps but have circular symmetry. Sectioning of the images allowed us to measure the step heights. The surface free energy was estimated from the growth step morphology. Molecular resolution was achieved for ferritin crystals, showing a hexagonal surface packing, as expected for the molecular lattice of a (111) face in a fcc crystal.

引用

页码：313 / 318

页数：5

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