title: Chemical cross-linking and H/D exchange for fast refinement of protein crystal structure.
abstract: A combination of chemical cross-linking and hydrogen-deuterium exchange coupled to high resolution mass spectrometry was used to describe structural differences of NKR-P1A receptor. The loop region extended from the compact core in the crystal structure was found to be closely attached to the protein core in solution. Our approach has potential to refine protein structures in solution within a few days and has very low sample consumption.
authors.forename: Daniel
authors.initials: D
authors.lastname: Rozbesky
authors.forename: Petr
authors.initials: P
authors.lastname: Man
authors.forename: Daniel
authors.initials: D
authors.lastname: Kavan
authors.forename: Josef
authors.initials: J
authors.lastname: Chmelik
authors.forename: Jiri
authors.initials: J
authors.lastname: Cerny
authors.forename: Karel
authors.initials: K
authors.lastname: Bezouska
authors.forename: Petr
authors.initials: P
authors.lastname: Novak
mesh_terms: D003432:Cross-Linking Reagents / Q000494:pharmacology*; D018360:Crystallography, X-Ray; D041961:Deuterium Exchange Measurement; D006801:Humans; D013058:Mass Spectrometry; D008958:Models, Molecular; D015394:Molecular Structure; D055651:NK Cell Lectin-Like Receptor Subfamily B / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D003432:Cross-Linking Reagents; C527203:KLRB1 protein, human; D055651:NK Cell Lectin-Like Receptor Subfamily B