title: Crystallization and preliminary crystallographic studies of trichomaglin, a novel ribosome-inactivating protein.
abstract: Trichomaglin, a novel ribosome-inactivating protein, has been crystallized in two crystal forms using the hanging-drop vapour-diffusion method. The form A and form B crystals belong to the orthorhombic space group P2(1)2(1)2(1) and the hexagonal space group P6(1) (or P6(5)), respectively. X-ray data have been collected to 3.3 and 2.2 A resolution for the form A and B crystals, respectively.
authors.affiliation: State Key Laboratory of Bio-organic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, People's Republic of China.
authors.forename: J
authors.initials: J
authors.lastname: Wu
authors.forename: J H
authors.initials: JH
authors.lastname: Gan
authors.forename: Z X
authors.initials: ZX
authors.lastname: Xia
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D009699:N-Glycosyl Hydrolases / Q000737:chemistry* / Q000494:pharmacology; D010940:Plant Proteins; D054789:Ribosome Inactivating Proteins, Type 1; D012270:Ribosomes / Q000187:drug effects*
chemical_list: D010940:Plant Proteins; D054789:Ribosome Inactivating Proteins, Type 1; D009699:N-Glycosyl Hydrolases; C119173:trichomaglin