Crystallization and preliminary X-ray diffraction study of the endo-polygalacturonase from Fusarium moniliforme.
Endo-polygalacturonases catalyze the fragmentation and solubilization of the homogalacturonan of the plant cell wall. These enzymes are extracellularly targeted glycoproteins produced by a number of organisms such as fungi, bacteria and plants, and are involved in both pathological and physiological processes. Single crystals of the endo-polygalacturonase from the phytopathogenic fungus Fusarium moniliforme were obtained by the vapour-diffusion method at 294 K. The starting material as well as the crystal consist of three forms with different degrees of glycosylation. The crystals belong to the orthorhombic space group P212121 and diffract to 1.9 A resolution on a synchrotron-radiation source under cryocooling conditions.
Dipartimento di Scienze Biochimiche e Centro di Biologia Molecolare del CNR, Piazzale Aldo Moro 5, 00185 Roma, Italy.
L
L
Federici
B
B
Mattei
C
C
Caprari
C
C
Savino
F
F
Cervone
D
D
Tsernoglou
D003460:Crystallization; D018360:Crystallography, X-Ray; D005615:Freezing; D005670:Fusarium / Q000201:enzymology*; D011096:Polygalacturonase / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D011096:Polygalacturonase