title: Crystallization and preliminary X-ray diffraction studies of a beta-carbonic anhydrase from the red alga Porphyridium purpureum.
abstract: The beta-carbonic anhydrase from the red alga Porphyridium purpureum was heterologously expressed, purified and crystallized. The crystals belong to space group P2(1) (unit-cell parameters a = 63.8, b = 113.9, c = 73.8 A, beta = 104.1 degrees) with two subunits per asymmetric unit and diffract to 2.5 A resolution.
authors.affiliation: Marine Biotechnology Institute, Kamaishi Laboratories, 3-75-1, Heita, Kamaishi, Iwate 026-0001, Japan. mitsuhashi@kamaishi.mbio.co.jp
authors.forename: S
authors.initials: S
authors.lastname: Mitsuhashi
authors.forename: T
authors.initials: T
authors.lastname: Mizushima
authors.forename: E
authors.initials: E
authors.lastname: Yamashita
authors.forename: S
authors.initials: S
authors.lastname: Miyachi
authors.forename: T
authors.initials: T
authors.lastname: Tsukihara
mesh_terms: D002256:Carbonic Anhydrases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D007527:Isoenzymes / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D010957:Plasmids / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D000461:Rhodophyta / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D007527:Isoenzymes; D011994:Recombinant Proteins; D002256:Carbonic Anhydrases