title: Crystallization and preliminary X-ray analysis of aspartate racemase from Pyrococcus horikoshii OT3.
abstract: Aspartate racemase from Pyrococcus horikoshii OT3 (P. AspR) has been crystallized in three crystal forms by the sitting-drop vapour-diffusion method. The crystals belong to the space groups P2(1), P2(1)2(1)2(1) and P3(1)21 (or P3(2)21). The crystals of space group P2(1) diffract X-rays beyond 1.7 A resolution under 90 K liquid-nitrogen cryoconditions with synchrotron radiation and were selected for structure determination. Two heavy-atom derivatives of this crystal form were obtained by the soaking method, which afforded the initial electron-density map.
authors.affiliation: Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: L
authors.initials: L
authors.lastname: Liu
authors.forename: K
authors.initials: K
authors.lastname: Iwata
authors.forename: Y
authors.initials: Y
authors.lastname: Kawarabayasi
authors.forename: H
authors.initials: H
authors.lastname: Kikuchi
authors.forename: A
authors.initials: A
authors.lastname: Kita
authors.forename: M
authors.initials: M
authors.lastname: Yohda
authors.forename: K
authors.initials: K
authors.lastname: Miki
mesh_terms: D000591:Amino Acid Isomerases / Q000737:chemistry*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D019711:Pyrococcus / Q000201:enzymology*
chemical_list: D000591:Amino Acid Isomerases; C019749:aspartate racemase