title: Expression, purification, crystallization and preliminary X-ray analysis of human argininosuccinic acid lyase.
abstract: Human argininosuccinic acid lyase (ASAL) has been expressed, purified and crystallized in several distinct crystal morphologies. At present only one form is suitable for X-ray diffraction analysis. These crystals grow as hexagonal prisms, with unit cell dimensions a = b = 104.6 A, c = 185.3 A and alpha = beta = 90 degrees, gamma = 120 degrees. The crystals exhibit the symmetry of space group P3(1)21 or its enantiomorph, P3(2)21 (indistinguishable crystallographically) and diffract to a minimum d-spacing of approximately 3.5 A.
authors.affiliation: Department of Biochemistry Research, Hospital for Sick Children, Toronto, Ontario, Canada.
authors.forename: M A
authors.initials: MA
authors.lastname: Turner
authors.forename: A M
authors.initials: AM
authors.lastname: Achyuthan
authors.forename: M S
authors.initials: MS
authors.lastname: Hershfield
authors.forename: R R
authors.initials: RR
authors.lastname: McInnes
authors.forename: P L
authors.initials: PL
authors.lastname: Howell
mesh_terms: D001123:Argininosuccinate Lyase / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D006801:Humans; D005810:Multigene Family; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D011994:Recombinant Proteins; D001123:Argininosuccinate Lyase