title: Protein crystals as scanned probes for recognition atomic force microscopy.
abstract: Lysozyme crystal growth has been localized at the tip of a conventional silicon nitride cantilever through seeded nucleation. After cross-linking with glutaraldehyde, lysozyme protein crystal tips image gold nanoparticles and grating standards with a resolution comparable to that of conventional tips. Force spectra between the lysozyme crystal tips and surfaces covered with antilysozyme reveal an adhesion force that drops significantly upon blocking with free lysozyme, thus confirming that lysozyme crystal tips can detect molecular recognition interactions.
authors.affiliation: Department of Physics & Astronomy, 6100 Main Street, Rice University, Houston, Texas, USA.
authors.forename: Nissanka S
authors.initials: NS
authors.lastname: Wickremasinghe
authors.forename: Jason H
authors.initials: JH
authors.lastname: Hafner
mesh_terms: D015374:Biosensing Techniques / Q000295:instrumentation / Q000379:methods; D003460:Crystallization / Q000379:methods*; D018625:Microscopy, Atomic Force; D015336:Molecular Probe Techniques; D015335:Molecular Probes / Q000737:chemistry*; D009113:Muramidase / Q000032:analysis* / Q000737:chemistry* / Q000648:ultrastructure; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D036103:Nanotechnology / Q000295:instrumentation / Q000379:methods; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000295:instrumentation / Q000379:methods*
chemical_list: D015335:Molecular Probes; D009113:Muramidase