Literature summary for 3.1.1.72 extracted from

Lansky, S.; Alalouf, O.; Solomon, V.; Alhassid, A.; Govada, L.; Chayen, N.E.; Chayan, N.E.; Belrhali, H.; Shoham, Y.; Shoham, G.
Crystallization and preliminary crystallographic analysis of Axe2, an acetylxylan esterase from Geobacillus stearothermophilus (2013), Acta Crystallogr. Sect. F, 69, 430-434.

Cloned(Commentary)

Cloned (Comment)	Organism
gene axe2, expression in Escherichia coli strain B834(DE3) for synthesis of a selenomethionine-labeled enzyme, and in strain BL21(DE3) for synthesis of the wild-type enzyme	Geobacillus stearothermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant wild-type and selenomethionine-labeled enzyme, mixing of 0.0025 ml of 3-6 mg/ml protein solution with 0.0025 ml of reservoir solution, and equilibration against 1 ml of reservoir solution, 4 different conditions resulting in four different crystal forms, best conditions are obtained with 6 mg/ml protein and 1.2 M K tartrate, 0.3 M NaCl, 0.1 M imidazole buffer, pH 7.2, 1-3 days, X-ray diffraction structure determination and analysis at 1.70-1.85 A resolution, three-dimensional structure determination	Geobacillus stearothermophilus

Crystallization (Comment)

Organism

purified recombinant wild-type and selenomethionine-labeled enzyme, mixing of 0.0025 ml of 3-6 mg/ml protein solution with 0.0025 ml of reservoir solution, and equilibration against 1 ml of reservoir solution, 4 different conditions resulting in four different crystal forms, best conditions are obtained with 6 mg/ml protein and 1.2 M K tartrate, 0.3 M NaCl, 0.1 M imidazole buffer, pH 7.2, 1-3 days, X-ray diffraction structure determination and analysis at 1.70-1.85 A resolution, three-dimensional structure determination

Geobacillus stearothermophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	Q09LX1	gene axe2	-
Geobacillus stearothermophilus T-6	Q09LX1	gene axe2	-

Synonyms

Synonyms	Comment	Organism
Axe2	-	Geobacillus stearothermophilus

General Information

General Information	Comment	Organism
physiological function	acetylxylan esterases hydrolyse the ester linkages of the xylan acetyl groups and thus improve the ability of main-chain hydrolysing enzymes to break down the sugar backbone units. As such, these enzymes play an important part in the hemi-cellulolytic utilization system of many microorganisms that use plant biomass for growth	Geobacillus stearothermophilus