3.2.1.145: galactan 1,3-beta-galactosidase
This is an abbreviated version!
For detailed information about galactan 1,3-beta-galactosidase, go to the full flat file.
Word Map on EC 3.2.1.145
-
3.2.1.145
-
glycoside
-
galactose
-
oligosaccharide
-
carbohydrate-binding
-
phanerochaete
-
exo-acting
-
chrysosporium
-
larch
-
beta-1,6-linked
-
arabinofuranose
-
thermocellum
-
dockerin
-
arabinogalactan-proteins
-
pectic
-
beta-1,3-linkage
-
avermitilis
-
galactooligosaccharides
-
analysis
- 3.2.1.145
- glycoside
- galactose
- oligosaccharide
-
carbohydrate-binding
-
phanerochaete
-
exo-acting
-
chrysosporium
-
larch
-
beta-1,6-linked
- arabinofuranose
- thermocellum
-
dockerin
- arabinogalactan-proteins
-
pectic
-
beta-1,3-linkage
- avermitilis
- galactooligosaccharides
- analysis
Reaction
Synonyms
arabinogalactan endo-1,3-beta-galactosidase, BbGal43A, beta-galactanase, Bl1,3Gal, Bl1,6Gal, BLLJ_1840, Ct1,3Gal43A, Cthe_0661, exo-/beta-1,3-galactanase, Exo-1,3-Gal, exo-beta-(1,3)-D-galactanase, exo-beta-(1->3)-D-galactanase, exo-beta-1,3-D -galactanase, exo-beta-1,3-D-galactanase, exo-beta-1,3-galactanase, exo-beta-1,6-galactobiohydrolase, Fo/1,3Gal, GH30_5 exo-beta-1,6-galactobiohydrolase, GH43_24 exo-beta-1,3-galactanase, Il1,3Gal, More, Pc1,3Gal43A, RsBGAL1, Sa1,3Gal43A, SGalase1, SGalase2
ECTree
Advanced search results
Crystallization
Crystallization on EC 3.2.1.145 - galactan 1,3-beta-galactosidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
purified recombinant His-tagged wild-type and selenomethionine-labeled enzymes in complex with galactose, IPTG, galactan, and lactose, hanging drop vapor diffusion method, mixing of 0.001 ml of 50 mg/ml protein in a buffer containing 20 mM Tris-HCl, pH 8.0, and 100 mM NaCl, with 0.001 ml of reservoir solution containing 100 mM sodium acetate, pH 4.5, and 2.9-3.3 M sodium chloride,16°C, 3 days, X-ray diffraction structure determination and analysis at 2.7-3.2 A resolution
purified recombinant enzyme, vapour diffusion method, mixing of 0.001 ml of 80 mg/ml protein in 0.02 M HEPES, pH 7.5, and 0.15 M NaCl, with 0.001 ml of reservoir solution containing 0.05 M calcium chloride dihydrate,0.1 M bis-Tris pH 6.5, 30% v/v polyethylene glycol monomethyl ether 550, and equilibration against 80.00 ml of reservoir solution, 17°C, X-ray diffraction structure determination and analysis at 1.4 A resolution, molecular replacement using using domain I of the Bacteroides thetaiotaomicron glycosyl hydrolase as search model, PDB ID 3nqh, modelling
selenomethionine-labeled recombinant Pc1,3Gal43A, hanging-drop vapour-diffusion method, 25°C, the reservoir solution contains 16% w/v PEG 10000, 95 mM ammonium sulfate, 95 mM Bis-Tris, pH 5.5, and 4.8% v/v glycerol, 3-10 days, X-ray diffraction structure determination and analysis at 1.8 A resolution, multiwavelength anomalous dispersion method, since molecular replacement is unsuccessful
-