Small-angle scattering and its interplay with crystallography, contrast variation in SAXS and SANS.
Methods of contrast variation are tools that are essential in macromolecular structure research. Anomalous dispersion of X-ray diffraction is widely used in protein crystallography. Recent attempts to extend this method to native resonant labels like sulfur and phosphorus are promising. Substitution of hydrogen isotopes is central to biological applications of neutron scattering. Proton spin polarization considerably enhances an existing contrast prepared by isotopic substitution. Concepts and methods of nuclear magnetic resonance (NMR) become an important ingredient in neutron scattering from dynamically polarized targets.
D001436:Bacteriorhodopsins / Q000737:chemistry; D054303:HIV Reverse Transcriptase / Q000737:chemistry; D006593:Hexokinase / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D008958:Models, Molecular; D033363:Neutron Diffraction / Q000379:methods*; D009707:Nucleosomes / Q000737:chemistry; D010743:Phospholipids / Q000737:chemistry; D018717:Purple Membrane / Q000737:chemistry; D012367:RNA, Viral / Q000737:chemistry; D054680:Ribosome Subunits, Small, Bacterial / Q000737:chemistry; D053838:Scattering, Small Angle; D025641:Tobacco necrosis satellite virus / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry; D014961:X-Ray Diffraction / Q000379:methods*
D009707:Nucleosomes; D010743:Phospholipids; D012367:RNA, Viral; D001436:Bacteriorhodopsins; D006593:Hexokinase; C514824:reverse transcriptase, Human immunodeficiency virus 1; D054303:HIV Reverse Transcriptase; D014357:Trypsin