title: Crystals of beta-xylanase from Aspergillus oryzae.
abstract: An endo-xylanase was isolated from the culture of fungus Aspergillus oryzae variant D5. The purified enzyme had a molecular weight of 24,000 and the isoelectric point of 3.6. Xylanase crystals were obtained from a polyethylene glycol 6000 solution by the hanging-drop method. Seeding was used for the enlargement of the crystal size. Crystals belong to the monoclinic space group P2(1) with cell dimensions a = 54.9 A, b = 74.5 A, c = 50.8 A, and beta = 108.7 degrees. Crystals diffract beyond 2.5 A resolution.
authors: Petersburg Nuclear Physics Institute, Gatchina, St Petersburg, Russia.
authors: A M
authors: AM
authors: Golubev
authors: Kilimnik AYu
authors: K N
authors: KN
authors: Neustroev
authors: R W
authors: RW
authors: Pickersgill
mesh_terms: D001236:Aspergillus oryzae / Q000201:enzymology*; D003460:Crystallization; D043364:Endo-1,4-beta Xylanases; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D011092:Polyethylene Glycols
chemical_list: D011092:Polyethylene Glycols; D006026:Glycoside Hydrolases; D043364:Endo-1,4-beta Xylanases