Sampling effects influence heights measured with atomic force microscopy

被引：11

作者：

Heymann, JB

Möller, C

Müller, DJ

机构：

[1] Max Planck Inst Mol Cell Biol & Genet, D-01307 Dresden, Germany

[2] NIAMS, LSBR, NIH, Bethesda, MD 20892 USA

[3] Tech Univ Dresden, BIOTEC, Dresden, Germany

来源：

JOURNAL OF MICROSCOPY-OXFORD | 2002年 / 207卷 / 01期

关键词：

AFM; Nyquist theorem; membrane; protein; resolution;

D O I：

10.1046/j.1365-2818.2002.01039.x

中图分类号：

TH742 [显微镜];

学科分类号：

摘要：

The atomic force microscope (AFM) is an exquisitely delicate probe measuring the height of a specimen at discrete sampling points in a fixed two-dimensional (2D) raster. The resulting topograph is a 2D digital image, with each pixel representing a distinct height measurement. The height of an object is determined as the average of the maximum heights measured above the supporting surface. We show that such object heights derived from a variety of organic samples depend critically on the sampling or pixel size of the 2D raster. It is concluded that to obtain accurate specimen heights, the pixel size must be small enough to resolve submolecular structures and thus ensure representative sampling of the height variation on the surface.

引用

页码：43 / 51

页数：9

共 54 条

[1] Protein, lipid and water organization in bacteriorhodopsin crystals:: a molecular view of the purple membrana at 1.9 Å resolution [J].