ArticleActa crystallographica. Section D, Biological crystallography2012
Modeling the SHG activities of diverse protein crystals.
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed.
- High-Throughput Screening to Obtain Crystal Hits for Protein Crystallography.Journal of visualized experiments : JoVE · 2023Article
- Stokes polarimetry-based second harmonic generation microscopy for collagen and skeletal muscle fiber characterization.Lasers in medical science · 2021Article
- Integrated sample-handling and mounting system for fixed-target serial synchrotron crystallography.Acta crystallographica. Section D, Structural biology · 2021Article
- Article
- Rapid screening ofJournal of applied crystallography · 2020Article
- Study of the Expression Transition of Cardiac Myosin Using Polarization-Dependent SHG Microscopy.Biophysical journal · 2020Article
- Imaging the Nonlinear Susceptibility Tensor of Collagen by Nonlinear Optical Stokes Ellipsometry.Biophysical journal · 2016Article
- Characterization of Protein Nanocrystals Based on the Reversibility of Crystallization.Crystal growth & design · 2016Article
- Second harmonic generation correlation spectroscopy for characterizing translationally diffusing protein nanocrystals.Acta crystallographica. Section D, Structural biology · 2016Article
- Guiding synchrotron X-ray diffraction by multimodal video-rate protein crystal imaging.Journal of synchrotron radiation · 2016Article
- Intercalating dyes for enhanced contrast in second-harmonic generation imaging of protein crystals.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Integrated nonlinear optical imaging microscope for on-axis crystal detection and centering at a synchrotron beamline.Journal of synchrotron radiation · 2013Article
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Abstract
A symmetry-additive ab initio model for second-harmonic generation (SHG) activity of protein crystals was applied to assess the likely protein-crystal coverage of SHG microscopy. Calculations were performed for 250 proteins in nine point-group symmetries: a total of 2250 crystals. The model suggests that the crystal symmetry and the limit of detection of the instrument are expected to be the strongest predictors of coverage of the factors considered, which also included secondary-structural content and protein size. Much of the diversity in SHG activity is expected to arise primarily from the variability in the intrinsic protein response as well as the orientation within the crystal lattice. Two or more orders-of-magnitude variation in intensity are expected even within protein crystals of the same symmetry. SHG measurements of tetragonal lysozyme crystals confirmed detection, from which a protein coverage of ~84% was estimated based on the proportion of proteins calculated to produce SHG responses greater than that of tetragonal lysozyme. Good agreement was observed between the measured and calculated ratios of the SHG intensity from lysozyme in tetragonal and monoclinic lattices.
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