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Title: Crystallization and preliminary X-ray crystallographic analysis of chitinase from barley seeds. Author: Song HK, Hwang KY, Kim KK, Suh SW. Journal: Proteins; 1993 Sep; 17(1):107-9. PubMed ID: 8234240. Abstract: Chitinase from barley seeds has been crystallized at room temperature using polyethylene glycol as precipitant. The crystal is monoclinic, belonging to the space group P2(1), with unit cell parameters of a = 69.43 A, b = 44.55 A, c = 81.41 A, and beta = 111.95 degrees. The asymmetric unit seems to contain two molecules of chitinase with a corresponding crystal volume per protein mass (VM) of 2.25 A3/Da and a solvent content of 45% by volume. The crystal diffracts to at least 2.0 A with X-rays from a rotating anode source and is very stable in the X-ray beam. X-ray data have been collected to better than 2.2 A Bragg spacing from a native crystal.[Abstract] [Full Text] [Related] [New Search]