Crystallization and preliminary X-ray analysis of a family 19 glycosyl hydrolase from Carica papaya latex.
A chitinase isolated from the latex of the tropical species Carica papaya has been purified to homogeneity and crystallized. This enzyme belongs to glycosyl hydrolase family 19 and exhibits exceptional resistance to proteolysis. The initially observed crystals, which diffracted to a resolution of 2.0 A, were improved through modification of the crystallization protocol. Well ordered crystals were subsequently obtained using N-acetyl-D-glucosamine, the monomer resulting from the hydrolysis of chitin, as an additive to the crystallization solution. Here, the characterization of a chitinase crystal that belongs to the monoclinic space group P2(1), with unit-cell parameters a = 69.08, b = 44.79, c = 76.73 A, beta = 95.33 degrees and two molecules per asymmetric unit, is reported. Diffraction data were collected to a resolution of 1.8 A. Structure refinement is currently in progress.
Huet
Joëlle
J
Laboratoire de Chimie Générale (CP 206/4), Institut de Pharmacie, Université Libre de Bruxelles (ULB), Campus de la Plaine, Boulevard du Triomphe, B-1050 Bruxelles, Belgium. jhuet@ulb.ac.be
Azarkan
Mohamed
M
Looze
Yvan
Y
Villeret
Vincent
V
Wintjens
René
R
D000117:Acetylglucosamine / Q000378:metabolism; D029441:Carica / Q000201:enzymology*; D002688:Chitinases / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D007840:Latex / Q000737:chemistry*; D009699:N-Glycosyl Hydrolases / Q000737:chemistry* / Q000302:isolation & purification
D007840:Latex; D002688:Chitinases; D009699:N-Glycosyl Hydrolases; D000117:Acetylglucosamine