TY - JOUR
T1 - From nano to subnano resolution
T2 - Reconstitution of hydrofobin structure from a SPM scan of HFBI layer
AU - Ruprecht, V.
AU - Paananen, Arja
AU - Torkkeli, M.
AU - Kyriakopoulos, F.
AU - Müllner, M.
AU - Pastushenko, V.
PY - 2008
Y1 - 2008
N2 - Applying Scanning Probe Microscopy (SPM) methods to determine structural details of biomolecules (e.g. proteins)
is one of the key trends in nanotechnology. Here we present the analysis of a Langmuir-Blodgett film of hydrofobin
HFBI. The statistical analysis is based on an accurate procedure of data detrending to study the quasi-crystalline clusters
of the HFBI layer. A statistical improvement method of signal to noise ratio was used. It relies on the variation of the
crystallographic lattice superimposed on a quasi-periodical data set. The procedure produces optimal values of crystallographic
periods and orientations of the symmetry axes. This information is used for selecting coherent data sets within a
crystallographic cluster. Superposition of cells from the same cluster and calculation of an average periodical structure
improves the signal to noise ratio, which leads from nano to subnano resolution of the protein structure. The number of
superimposed cells N defines the resolution gain factor N1/2. In the case of hydrofobin, the value of N lies in the range of
25-100. This allows for the determination of fine structural details of HFBI. Average structures obtained from different
domains of the protein layer also show a high degree of reproducibility.
AB - Applying Scanning Probe Microscopy (SPM) methods to determine structural details of biomolecules (e.g. proteins)
is one of the key trends in nanotechnology. Here we present the analysis of a Langmuir-Blodgett film of hydrofobin
HFBI. The statistical analysis is based on an accurate procedure of data detrending to study the quasi-crystalline clusters
of the HFBI layer. A statistical improvement method of signal to noise ratio was used. It relies on the variation of the
crystallographic lattice superimposed on a quasi-periodical data set. The procedure produces optimal values of crystallographic
periods and orientations of the symmetry axes. This information is used for selecting coherent data sets within a
crystallographic cluster. Superposition of cells from the same cluster and calculation of an average periodical structure
improves the signal to noise ratio, which leads from nano to subnano resolution of the protein structure. The number of
superimposed cells N defines the resolution gain factor N1/2. In the case of hydrofobin, the value of N lies in the range of
25-100. This allows for the determination of fine structural details of HFBI. Average structures obtained from different
domains of the protein layer also show a high degree of reproducibility.
U2 - 10.2174/1874140100802010006
DO - 10.2174/1874140100802010006
M3 - Article
SN - 1874-1401
VL - 2
SP - 6
EP - 11
JO - The Open Nanoscience Journal
JF - The Open Nanoscience Journal
ER -