Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea.
Recombinant amylosucrase from Neisseria polysaccharea was crystallized by the vapour-diffusion procedure in the presence of polyethylene glycol 6000. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 95.7, b = 117.2, c = 62.1 A, and diffract to 1.6 A resolution. A p-chloromercuribenzene sulfonate (pcmbs) derivative has been identified and a selenomethionine-substituted protein has been produced and crystallized.
Skov
L K
LK
Protein Structure Group, Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark.
Mirza
O
O
Henriksen
A
A
Potocki de Montalk
G
G
Remaud-Simeon
M
M
Sarcabal
P
P
Willemot
R M
RM
Monsan
P
P
Gajhede
M
M
D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D002942:Circular Dichroism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology; D005964:Glucosyltransferases / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D009343:Neisseria / Q000201:enzymology*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D005964:Glucosyltransferases; C019700:amylosucrase