SCANNING FORCE MICROSCOPY OF ESCHERICHIA-COLI OMPF PORIN IN BUFFER SOLUTION

被引：10

作者：

SCHABERT, FA

HOH, JH

KARRASCH, S

HEFTI, A

ENGEL, A

机构：

来源：

JOURNAL OF VACUUM SCIENCE & TECHNOLOGY B | 1994年 / 12卷 / 03期

关键词：

D O I：

10.1116/1.587273

中图分类号：

TM [电工技术]; TN [电子技术、通信技术];

学科分类号：

0808 ; 0809 ;

摘要：

The extracellular and periplasmic surface topography of the E. coli outer membrane protein OmpF reconstituted into 2D crystals in the presence of phospholipids were investigated with a scanning force microscope in buffer solution. Topographs exhibiting 2 nm lateral resolution are in good agreement with data from electron microscopy and x-ray crystallography, and indicate the exciting possibility to monitor structural changes of ''live systems'' at molecular resolution by scanning force microscopy.

引用

页码：1504 / 1507

页数：4

共 50 条

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[7] REGULATED OMPF PORIN SYNTHESIS IN ESCHERICHIA-COLI K-12
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[8] TRIMERIZATION OF AN INVITRO SYNTHESIZED OMPF PORIN OF ESCHERICHIA-COLI OUTER-MEMBRANE
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[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1991, 266 (17) : 11295 - 11300
[9] INTERACTION OF AMINOGLYCOSIDES WITH THE OUTER MEMBRANES AND PURIFIED LIPOPOLYSACCHARIDE AND OMPF PORIN OF ESCHERICHIA-COLI
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[10] REPRODUCIBLE ACQUISITION OF ESCHERICHIA-COLI PORIN SURFACE TOPOGRAPHS BY ATOMIC-FORCE MICROSCOPY
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