title: Purification, crystallization and preliminary X-ray analysis of an acetylxylan esterase from Bacillus pumilus.
abstract: The gene encoding for acetylxylan esterase from Bacillus pumilus has been cloned and expressed in Escherichia coli. The recombinant protein has been purified to homogeneity and crystallized. The crystals obtained are of regular shape of dimensions 0.05 x 0.05 x 0.05 mm with R32 symmetry and diffract to 2.0 A using synchrotron radiation.
authors.affiliation: International Centre for Genetic Engineering and Biotechnology, Area Science Park, Padriciano 99, I-34012 Trieste, Italy. benini@icgeb.trieste.it
authors.forename: S
authors.initials: S
authors.lastname: Benini
authors.forename: G
authors.initials: G
authors.lastname: Degrassi
authors.forename: I
authors.initials: I
authors.lastname: Krastanova
authors.forename: D
authors.initials: D
authors.lastname: Lamba
authors.forename: V
authors.initials: V
authors.lastname: Venturi
mesh_terms: D000115:Acetylesterase / Q000737:chemistry* / Q000235:genetics; D001407:Bacillus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D011994:Recombinant Proteins; D000115:Acetylesterase; C081851:acetylxylan esterase