Crystallization and preliminary X-ray diffraction studies of beta-cryptogein, a toxic elicitin secreted by the phytopathogenic fungus Phytophthora cryptogea.
Crystals of the basic elicitin secreted by Phytophthora cryptogea have been obtained by the hanging-drop method of vapor diffusion from sodium chloride solutions. The crystals belong to the tetragonal space group P4(1)22 (or enantiomorph P4(3)22), with unit cell dimensions a = b = 47 A, c = 137 A and probably contain two molecules per asymmetric unit. The crystals are very stable to X-rays and diffract to 2.2 A resolution on a synchrotron radiation source.
Guilloteau
J P
JP
Laboratoire d'Etude des Protéines, INRA-Versailles, France.
Nespoulous
C
C
Huet
J C
JC
Beauvais
F
F
Pernollet
J C
JC
Brunie
S
S
D020418:Algal Proteins; D003460:Crystallization; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D010838:Phytophthora / Q000737:chemistry*; D014961:X-Ray Diffraction
D020418:Algal Proteins; D005656:Fungal Proteins; C061032:cryptogein protein, Phytophthora cryptogea