Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 9 (September 2007)

crystallization communications

Acta Cryst. (2007). F63, 737-739 [ doi:10.1107/S1744309107034793 ]

Crystallization 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

T. Miyakawa, Y. Sawano, K. Miyazono, K. Hatano and M. Tanokura

Abstract: 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 P2₁3, with unit-cell parameters a = b = c = 143.2 Å.

Keywords: ginkbilobin-2; antifungal proteins; Ginkgo biloba.