title: Purification, characterization and preliminary crystallographic studies of a PR-10 protein from Pachyrrhizus erosus seeds.
abstract: A 16 kDa protein SPE16 was purified from the seeds of Pachyrrhizus erosus. Its N-terminal amino-acid sequence showed significant sequence homology to pathogenesis-related proteins from the PR-10 family. An activity assay indicated that SPE16 possesses ribonuclease activity as do some other PR-10 proteins. SPE16 crystals were obtained by the hanging-drop vapour-diffusion method. The space group is P2(1)2(1)2(1), with unit-cell parameters a = 53.36, b = 63.70, c = 72.96 A.
authors.affiliation: School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
authors.forename: Fang
authors.initials: F
authors.lastname: Wu
authors.forename: Yikun
authors.initials: Y
authors.lastname: Li
authors.forename: Shaojie
authors.initials: S
authors.lastname: Chang
authors.forename: Zhaocai
authors.initials: Z
authors.lastname: Zhou
authors.forename: Fang
authors.initials: F
authors.lastname: Wang
authors.forename: Xiaomin
authors.initials: X
authors.lastname: Song
authors.forename: Yujuan
authors.initials: Y
authors.lastname: Lin
authors.forename: Weimin
authors.initials: W
authors.lastname: Gong
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D029905:Pachyrhizus / Q000196:embryology*; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification*; D011487:Protein Conformation; D012639:Seeds / Q000737:chemistry*
chemical_list: D010940:Plant Proteins; C053376:pathogenesis-related proteins, plant