Electron crystallography of macromolecular periodic arrays on phospholipid monolayers |
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| Affiliation: | 1. Department of Chemical Immunology, Leiden University Medical Center (LUMC), Einthovenweg 20, 2333 ZC Leiden, The Netherlands;2. Department of Immunopathology, Sanquin Research and Landsteiner Laboratory, Academic Medical Center (AMC)/Universiteit van Amsterdam (UvA), Plesmanlaan 125, 1066 CX Amsterdam, The Netherlands;1. Department of Physiology, Northwestern University, Chicago, IL 60611, USA;2. Department of Psychiatry and Behavioral Sciences, Northwestern University, Chicago, IL 60611, USA;1. Physical Medicine and Rehabilitation Research-Copenhagen (PMR-C), Copenhagen University Hospital, Hvidovre, Kettegård allé 30, Hvidovre 2650, Denmark;2. Department of Physiotherapy, Copenhagen University Hospital, Hvidovre, Kettegård allé 30, Hvidovre 2650, Denmark;3. Department of Orthopaedic Surgery, Clinical Orthopaedic Research Hvidovre, Kettegård allé 30, Hvidovre 2650, Denmark;1. Department of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA;2. Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA;3. National Resource for Automated Molecular Microscopy, New York Structural Biology Center, New York, NY 10027, USA;4. Department of Molecular Physiology & Biophysics, Vanderbilt University, Nashville, TN 37212, USA;5. Department of Biochemistry, Vanderbilt University, Nashville, TN 37205, USA;1. College of Biological and Food Engineering, Guangdong University of Petrochemical Technology, Maoming 525000, China;2. College of Science, Heilongjiang Bayi Agricultural University, Daqing 163319, China |
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| Abstract: | Electron crystallography has the potential of yielding structural information equivalent to x-ray diffraction. The major difficulty has been preparing specimens with the required structural order and size for diffraction and imaging in the electron microscope. 2D crystallization on phospholipid monolayers is capable of fulfilling both of these requirements. Crystals can form as a result of specific interactions with a protein's ligand or an analog, suitably linked to a lipid tail; or on a surface of complementary head-group charge. With such choices, the availability of a suitable lipid is limited only by synthetic chemistry. Ultimately, it is the quality and regularity of the protein-protein interactions that determine the crystalline order, as it is with any protein crystal. In the case of streptavidin, the monolayer crystal diffracts beyond 2.5 Å. A 3 Å projection map reconstructed from electron diffraction amplitudes and phases from images shows density which can be interpreted as β-sheets and clusters of side chains. It remains to be shown that the monolayer crystals are flat and diffract as well at high tilt angle as untilted. Technological issues such as charging must be resolved. With parallel advances in data collection and processing, electron crystallography of monolayer macromolecular crystals will eventually take its place beside x-ray crystallography and NMR as a routine and efficient structural technique. |
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