Crystallization and preliminary crystallographic analysis of Axe2, an acetylxylan esterase from Geobacillus stearothermophilus. Corrigendum
نویسندگان
چکیده
Institute of Chemistry and the Laboratory for Structural Chemistry and Biology, Hebrew University of Jerusalem, Jerusalem 91904, Israel, Department of Biotechnology and Food Engineering, Technion – Israel Institute of Technology, Haifa 32000, Israel, Department of Surgery and Cancer, Imperial College London, London SW7 2AZ, England, and European Synchrotron Radiation Facility, BP 220, 38043 Grenoble, France
منابع مشابه
Purification, crystallization and preliminary X-ray analysis of an acetylxylan esterase from Bacillus pumilus.
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.
متن کاملCrystallization and preliminary crystallographic analysis of a thermostable family 52 beta-D-xylosidase from Geobacillus stearothermophilus T-6.
Beta-D-xylosidases (EC 3.2.1.37) are hemicellulases that hydrolyze short xylooligosaccharides into single xylose units. In this study, the first crystallization and preliminary X-ray analysis of a family 52 glycoside hydrolase, the beta-D-xylosidase (XynB2) from Geobacillus stearothermophilus T-6, is described. XynB2 is a dimeric protein consisting of two identical subunits of 705 amino acids w...
متن کاملPurification, crystallization and preliminary X-ray analysis of the M.BseCI DNA methyltransferase from Bacillus stearothermophilus.
The DNA methyltransferase M.BseC1 from B. stearothermophilus methylates the N6 atom of the 3' adenine in the sequence 5'-ATCGAT-3'. The 579-residue protein has been isolated and crystallized using seeding and microdialysis techniques. The crystals are monoclinic, space group P2(1) with cell dimensions a = 53.7, b = 85.7, c = 151.8 A and beta = 95.1 degrees, two molecules in the asymmetric unit ...
متن کاملMolecular Engineering of the Geobacillus stearothermophilus α-Amylase and Cel5E from Chlostridium thermocellim; In Silico Approach
Background: Considering natural thermal stability, Geobacillus stearothermophilus amylase and Cel5E from Clostridium thermocellum are good candidates for industrial applications. To be compatible with the industrial applications, this enzyme should be stable in the high temperatures, so any improvement in their thermal stability is valuable.Objectives: Us...
متن کاملIdentification, characterization and preliminary X-ray diffraction analysis of the rolling-circle replication initiator protein from plasmid pSTK1
Antibiotic resistance in bacterial pathogens poses an ever-increasing risk to human health. In antibiotic-resistant strains of Staphylococcus aureus this resistance often resides in extra-chromosomal plasmids, such as those of the pT181 family, which replicate via a rolling-circle mechanism mediated by a plasmid-encoded replication initiation protein. Currently, there is no structural informati...
متن کامل