Two-dimensional crystals of proteins on lipid layers
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Cited by (109)
Double-headed binding of myosin II to F-actin shows the effect of strain on head structure
2023, Journal of Structural BiologyStructural studies of the endogenous spliceosome – The supraspliceosome
2017, MethodsCitation Excerpt :We therefore tried a different approach of concentrating the particles on charged lipid monolayer films. This methodology has been successfully used in electron crystallography studies of biologically active complexes [58,59]. We adapted this method to reproducibly concentrate and generate, on a positively charged monolayer, a layer with a high density of supraspliceosomes that can be picked up on holey carbon grids, blotted and plunged into liquid ethane, and visualized in the frozen-hydrated state [36].
Assemblies of pore-forming toxins visualized by atomic force microscopy
2016, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :There are two approaches for preparing 2D assemblies of PFTs. The first is very similar to the techniques employed for the EM visualization of 2D protein crystals [81,82]. In this approach, a lipid monolayer is first transferred onto mica using the LB method; then, the mica-supported lipid monolayer is horizontally lowered onto a separately prepared lipid monolayer at the air/water interface, and the protein is injected into the subphase.
Electron crystallography - The waking beauty of structural biology
2012, Current Opinion in Structural BiologyEffect of surface chemistry of novel templates on crystallization of proteins
2012, Chemical Engineering ScienceCitation Excerpt :This means the crystallization of macromolecules will depend more on surface properties than small salt compounds. Attempts to find correlations between proteins and surfaces that can improve or just change their crystallization parameters are also recorded in the literature and different substrates have been used for this purpose—mineral surfaces (McPherson and Schilichta, 1988; Kimble et al., 1998), lipid films (Edwards et al., 1994; Kornberg and Darst, 1991; Kubo et al., 2007), polymers (Grzesiak and Matzger, 2008), protein thin film (Pechkova and Nicolini, 2001,2002), molecular imprinted polymer (Saridakis et al., 2011), as well as applying chemical modification of mica (Falini et al., 2002; Simone et al., 2006; Tang et al., 2005; Tosi et al., 2008) or glass surface (Liu et al., 2007; Nanev and Tsekova, 2000; Rong et al., 2002; Sun et al., 2010, Tsekova et al., 2002). Here we report the preparation of new surface chemical treated crystallization templates, the determination of their dispersive and polar surface energies components and crystallization performance of Lysozyme, Thaumatin, Catalase and Ferritin on them.
Membrane Crystallization Technology
2010, Comprehensive Membrane Science and Engineering