Expression, purification, crystallization and preliminary X-ray analysis of the iota-carrageenase from Alteromonas fortis.
This is the first crystallization report of a glycoside hydrolase which belongs to family 82. A recombinant form of His-tagged iota-carrageenase from Alteromonas fortis was expressed, purified and crystallized. Crystals were obtained by the vapour-diffusion method using polyethylene glycol (M(W) = 6000) as a precipitant. They belong to space group P2(1), with unit-cell parameters a = 56. 75, b = 91.04, c = 125.01 A, beta = 93.41 degrees. The unit cell contains two molecules in the asymmetric unit related by a non-crystallographic twofold axis. Crystals diffracted to 2.0 A resolution on a synchrotron beamline.
Michel
G
G
Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS/CEA, Grenoble, France.
Flament
D
D
Barbeyron
T
T
Vernet
T
T
Kloareg
B
B
Dideberg
O
O
D020591:Alteromonas / Q000201:enzymology* / Q000235:genetics; D001426:Bacterial Proteins; D002351:Carrageenan / Q000378:metabolism*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D006026:Glycoside Hydrolases / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D002351:Carrageenan; D006026:Glycoside Hydrolases; C019846:kappa-carrageenase protein, Alteromonadaceae