Purification, characterization and preliminary crystallographic studies of a PR-10 protein from Pachyrrhizus erosus seeds.
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.
Wu
Fang
F
School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Li
Yikun
Y
Chang
Shaojie
S
Zhou
Zhaocai
Z
Wang
Fang
F
Song
Xiaomin
X
Lin
Yujuan
Y
Gong
Weimin
W
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*
D010940:Plant Proteins; C053376:pathogenesis-related proteins, plant