On the negative straining of the protein crystal structure.
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.
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
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