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Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscope.

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Title: Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscope.
Authors: SCHEURING, S1, MÜLLER, D. J1, RINGLER, P1, HEYMANN, J. B1, ENGEL, A1
Source: Journal of Microscopy. Jan1999, Vol. 193 Issue 1, p28-35. 8p. 11 Black and White Photographs, 4 Diagrams, 1 Chart.
Subjects: Streptavidin, Crystals, Electron microscopy, Atomic models, X-ray crystallography
Abstract: Streptavidin crystals were grown on biotinylated lipid monolayers at an air/water interface and transferred onto highly oriented pyrolytic graphite (HOPG). These arrays could be imaged to a resolution below 1 nm using the atomic force microscope. The surface topographs obtained were compared with negative-stain electron microscopy images and the atomic model as determined by X-ray crystallography. The streptavidin tetramer (60 kDa) exposes two free biotin-binding sites to the buffer solution, while two are occupied by linkage to the lipid monolayer. Therefore, the streptavidin 2D crystals can be used as nanoscale matrices for binding biotinylated compounds. Furthermore, this HOPG-based preparation method provides a general novel approach to study the structure of protein arrays assembled on lipid monolayers with the AFM. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Microscopy is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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DbLabel: Engineering Source
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  Data: Imaging streptavidin 2D crystals on biotinylated lipid monolayers at high resolution with the atomic force microscope.
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Microscopy%22">Journal of Microscopy</searchLink>. Jan1999, Vol. 193 Issue 1, p28-35. 8p. 11 Black and White Photographs, 4 Diagrams, 1 Chart.
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  Data: <searchLink fieldCode="DE" term="%22Streptavidin%22">Streptavidin</searchLink><br /><searchLink fieldCode="DE" term="%22Crystals%22">Crystals</searchLink><br /><searchLink fieldCode="DE" term="%22Electron+microscopy%22">Electron microscopy</searchLink><br /><searchLink fieldCode="DE" term="%22Atomic+models%22">Atomic models</searchLink><br /><searchLink fieldCode="DE" term="%22X-ray+crystallography%22">X-ray crystallography</searchLink>
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  Data: Streptavidin crystals were grown on biotinylated lipid monolayers at an air/water interface and transferred onto highly oriented pyrolytic graphite (HOPG). These arrays could be imaged to a resolution below 1 nm using the atomic force microscope. The surface topographs obtained were compared with negative-stain electron microscopy images and the atomic model as determined by X-ray crystallography. The streptavidin tetramer (60 kDa) exposes two free biotin-binding sites to the buffer solution, while two are occupied by linkage to the lipid monolayer. Therefore, the streptavidin 2D crystals can be used as nanoscale matrices for binding biotinylated compounds. Furthermore, this HOPG-based preparation method provides a general novel approach to study the structure of protein arrays assembled on lipid monolayers with the AFM. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
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  Data: <i>Copyright of Journal of Microscopy is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1046/j.1365-2818.1999.00434.x
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      – Code: eng
        Text: English
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        Type: general
      – SubjectFull: Crystals
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      – SubjectFull: Electron microscopy
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      – SubjectFull: Atomic models
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      – SubjectFull: X-ray crystallography
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              Text: Jan1999
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              Y: 1999
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