Ordering in Lipid Monolayers Studied by Synchrotron X-Ray Diffraction and Fluorescence Microscopy

Kjaer, K.; Als‐Nielsen, J.; Helm, C. A.; Laxhuber, L. A.; Möwald, H.

doi:10.1103/physrevlett.59.744

Cited by 17 publications

(22 citation statements)

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“…Synchrotron grazing incidence x-ray diffraction experiments were performed using the liquid-surface diffractometer (Als-Nielsen and Mohwald, 1991; Kjaer et al, 1987) on the undulator beam line BW1 at HASYLAB, DESY, Hamburg. A sealed and thermostated Langmuir trough (135 X 80 X 16 mm3) with continuous Wilhelmy type pressure-measuring system was mounted on the diffractometer.…”

Section: Methodsmentioning

confidence: 99%

“…Because the latter technique is not free of artifacts and because the structure at the fluid interface has been shown to depend on environmental conditions, in situ diffraction studies of protein arrays are of utmost importance. Surface x-ray diffraction techniques have recently been developed to study lipid monolayers at air/water interfaces (Als-Nielsen and Mohwald, 1991;Kjaer et al, 1987). Extension of these techniques to investigate 2D protein crystals without staining, however, requires another step in instrumentation and surface control because of the Tel.…”

Section: Introductionmentioning

confidence: 99%

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X-ray diffraction of a protein crystal anchored at the air/water interface

Haas¹,

Brezesinski²,

Möhwald³

1995

Biophysical Journal

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We report the first successful in situ x-ray diffraction experiment with a 2D protein array at the lipid/water interface and demonstrate that the order can be controlled via lateral pressure or density. A protein (streptavidin) was bound to a monolayer of biotinylated lipid at the air/water interface, and diffraction of the protein layer could be measured to many orders. Compression of the monolayer changed the diffraction pattern drastically, indicating that the protein structure can be strongly influenced by external parameters like lateral pressure or density. From the width of the peaks, we find that aggregates consisting of as few as 100 monomers contribute to the diffraction. This indicates that the structure of even low order aggregates can be studied in situ. Grazing incidence diffraction can become a strong new method to study the crystallization and the interactions between proteins free from artifacts by staining or sample preparation.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

X-ray diffraction of a protein crystal anchored at the air/water interface

Haas¹,

Brezesinski²,

Möhwald³

1995

Biophysical Journal

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“…Data taken at various pressures above 7rc have been described recently (Kjaer et al, 1987) and are reproduced in Fig. 3 of this paper.…”

Section: (B) Fluorescence Microscopymentioning

confidence: 99%

“…To eliminate this latter drawback we have designed experiments to measure synchrotron x-ray diffraction from a monolayer at the air/water interface Kjaer et al, 1987). We report here comprehensively on our results for the phospholipid L-a-dimyristoyl phosphatidic acid (DMPA).…”

Section: Introductionmentioning

confidence: 99%

Phospholipid monolayers between fluid and solid states

Helm¹,

Möhwald²,

Kjær³

et al. 1987

Biophysical Journal

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184

107

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Monolayers of the phospholipid dimyristoyl phosphatidic acid on the surface of water have been studied by a combination of the new techniques of synchrotron x-ray diffraction and fluorescence microscopy with classical surface pressure data. The pressure vs. area isotherm changes slope at the surface pressures pi c and pi s. The optical technique demonstrates that between pi c and pi s the fluid phase coexists with a denser "gel" phase. Electron diffraction data have shown that the gel phase has bond orientational order over tens of micrometers. However, the x-ray data demonstrate that positional correlations extend only over tens of angstroms. Thus, the gel phase is not crystalline. Above pi s a solid phase is formed with a positional correlation range that is eight times longer for the chemically purest films.

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“…A vital branch of the imaging of waves is the so-called super-resolution imaging, including fluorescence microscopy (Kjaer etal. 1987; Sánchez, Novotny & Xie 1999), X-rays (Rodenburg etal. 2007; Miao etal.…”

Section: Introductionmentioning

confidence: 99%