title: On the negative straining of the protein crystal structure.
abstract: It has been shown that in some cases negative staining reveals structure with details down to 0.4 nm in size, the nature of protein playing a key role. Various stains seem to interact with different parts of a thermitase (a serine protease) molecule, which results in intensity changes in electron diffraction patterns.
mesh_terms: D003460:Crystallization; D010450:Endopeptidases; D008854:Microscopy, Electron; D009942:Organometallic Compounds; D010772:Phosphotungstic Acid; D012697:Serine Endopeptidases; D017640:Silicates; D012824:Silicic Acid; D013194:Staining and Labeling; D014414:Tungsten; D017973:Tungsten Compounds; D014501:Uranium
chemical_list: D009942:Organometallic Compounds; D017640:Silicates; D017973:Tungsten Compounds; D010772:Phosphotungstic Acid; D012824:Silicic Acid; C005460:uranyl acetate; D014501:Uranium; D010450:Endopeptidases; D012697:Serine Endopeptidases; C022728:thermitase; C021746:silicotungstic acid; D014414:Tungsten