Open AccessCrystallization and preliminary X‐ray analysis of ginkbilobin‐2 from Ginkgo biloba seeds: a novel antifungal protein with homology to the extracellular domain of plant cysteine‐rich receptor‐like kinases
Author(s) -
Miyakawa Takuya,
Sawano Yoriko,
Miyazono Kenichi,
Hatano Kenichi,
Tanokura Masaru
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107034793
Subject(s) - homology modeling , extracellular , ginkgo biloba , cysteine , homology (biology) , kinase , chemistry , biology , biochemistry , botany , gene , enzyme
The antifungal protein ginkbilobin‐2 (Gnk2) from Ginkgo biloba seeds does not show homology to other pathogenesis‐related proteins, but does show homology to the extracellular domain of plant cysteine‐rich receptor‐like kinases. Native Gnk2 purified from ginkgo nuts and the selenomethionine derivative of recombinant Gnk2 (SeMet‐rGnk2) were crystallized by the sitting‐drop vapour‐diffusion method using different precipitants. X‐ray diffraction data were collected from Gnk2 at 2.38 Å resolution and from SeMet‐rGnk2 at 2.79 Å resolution using a synchrotron‐radiation source. The crystals of both proteins belonged to the primitive cubic space group P 2 1 3, with unit‐cell parameters a = b = c = 143.2 Å.