Dresden 2017 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 5: Single Molecule Biophysics
BP 5.4: Vortrag
Montag, 20. März 2017, 16:00–16:15, HÜL 386
3D Light microscopy of protein structure with Angstrom resolution — •Daniel Böning1, Siegfried Weisenburger1, Benjamin Schomburg2, Karin Giller2, Stefan Becker2, Christian Griesinger2, and Vahid Sandoghdar1 — 1Max Planck Institute for the Science of Light, 91058 Erlangen, Germany — 2Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany
Insight into the atomic and molecular structure of proteins and other biomolecular assemblies is highly desirable in many areas of life sciences, and several physical techniques such as x-ray crystallography, electron microscopy (EM) and magnetic resonance spectroscopy have been employed over decades to arrive at such information. However, due to limitations in each method the structures of the great majority of the proteins and larger biomolecules remain unknown to us. Here, we present a novel optical microscopy technique, termed Cryogenic Optical Localization in three Dimensions (COLD), which reaches Angstrom resolution in deciphering the positions of several fluorescent sites within a single small protein. The key mechanism for reaching this limit is the enhanced photostability at low temperatures, thus providing a much higher shot-noise-limited signal-to-noise ratio than in room temperature super-resolution microscopy. As an example of the application of this method, we show how we resolve the four sites where biotin binds to streptavidin in three dimensions. COLD opens new doors for obtaining quantitative structure information from small to medium sized biomolecules at the Angstrom scale and can complement other existing techniques such as magnetic resonance spectroscopy.