Abstract
A recombinant form of His-tagged kappa-carrageenase from Pseudoalteromonas carrageenovora has been expressed, purified and crystallized. Crystals have been obtained by the vapour-diffusion method using polyethylene glycol (Mr = 4000) as a precipitant. These crystals belong to the space group P212121, with unit-cell parameters a = 58.2, b = 62.8, c = 77.9 A, and diffract to 2.2 A resolution on a rotating-anode X-ray source.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Bacterial Proteins / chemistry*
-
Bacterial Proteins / genetics
-
Bacterial Proteins / isolation & purification
-
Crystallization
-
Escherichia coli / genetics
-
Glycoside Hydrolases / chemistry*
-
Glycoside Hydrolases / genetics
-
Glycoside Hydrolases / isolation & purification
-
Gram-Negative Aerobic Bacteria / enzymology*
-
Gram-Negative Aerobic Bacteria / genetics
-
Recombinant Proteins / biosynthesis
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / isolation & purification
-
X-Ray Diffraction
Substances
-
Bacterial Proteins
-
Recombinant Proteins
-
Glycoside Hydrolases
-
kappa-carrageenase protein, Alteromonadaceae