Imaging of subunit complexes of thermophilic bacterium H(+)-ATPase with scanning tunneling microscopy.
Using a scanning tunneling microscope (STM), we observed reconstructed subunit complexes of H(+)-ATPase of a thermophilic bacterium. The measurement was carried out in air without conductive coating on the samples deposited on a highly oriented pyrolytic graphite (HOPG). The F1 subunit complex of the H(+)-ATPase, and an H(+)-ATPase whose F0 portion was embedded into liposomes prepared from soybean lecithin were imaged. Overall structural images of the subunit complex F1 were obtained: the structural dimensions of the STM images are in agreement with those deduced from conventional methods such as an transmission electron microscopy (TEM) and small-angle X-ray scattering (SAX) experimentation. Regarding the STM imaging of these samples, we discuss the advantages and disadvantages of the STM over those of conventional methods such as a TEM and SAX.
Masai
J
J
Research Center, Mitsubishi Kasei Corporation, Yokohama, Japan.
Shibata
T
T
Kagawa
Y
Y
Kondo
S
S
D003001:Cloning, Molecular; D004926:Escherichia coli; D037102:Lectins; D008081:Liposomes; D008854:Microscopy, Electron; D016252:Microscopy, Scanning Tunneling; D037121:Plant Lectins; D006180:Proton-Translocating ATPases / Q000235:genetics / Q000648:ultrastructure*; D030262:Soybean Proteins; D010835:Phytohemagglutinins
D037102:Lectins; D008081:Liposomes; D037121:Plant Lectins; D006180:Proton-Translocating ATPases; D030262:Soybean Proteins; C028824:soybean lectin; D010835:Phytohemagglutinins