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Expression, purification, crystallisation and preliminary X-ray diffraction analysis of Thermotoga neapolitana beta-glucosidase B

Turner, Pernilla LU ; Pramhed, Anna LU ; Kanders, Erik; Hedström, Martin LU ; Nordberg Karlsson, Eva LU and Logan, Derek LU (2007) In Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00 63(9). p.802-806
Abstract
-Glucosidases belong to families 1, 3 and 9 of the glycoside hydrolases and act on cello-oligosaccharides. Family 1 and 3 enzymes are retaining and are reported to have transglycosylation activity, which can be used to produce oligosaccharides and glycoconjugates. Family 3 enzymes are less well characterized than their family 1 homologues and to date only two crystal structures have been solved. Here, the expression, purification, crystallization and X-ray diffraction data of a family 3 -glucosidase from the hyperthermophilic bacterium Thermotoga neapolitana are reported. Crystals of selenomethionine-substituted protein have also been grown. The crystals belong to space group C2221, with unit-cell parameters a = 74.9, b = 127.0, c = 175.2... (More)
-Glucosidases belong to families 1, 3 and 9 of the glycoside hydrolases and act on cello-oligosaccharides. Family 1 and 3 enzymes are retaining and are reported to have transglycosylation activity, which can be used to produce oligosaccharides and glycoconjugates. Family 3 enzymes are less well characterized than their family 1 homologues and to date only two crystal structures have been solved. Here, the expression, purification, crystallization and X-ray diffraction data of a family 3 -glucosidase from the hyperthermophilic bacterium Thermotoga neapolitana are reported. Crystals of selenomethionine-substituted protein have also been grown. The crystals belong to space group C2221, with unit-cell parameters a = 74.9, b = 127.0, c = 175.2 Å. Native data have been collected to 2.4 Å resolution and the structure has been solved to 2.7 Å using the selenomethionine MAD method. Model building and refinement of the structure are under way. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
multiple-wavelength anomalous dispersion., selenomethionine incorporation, Thermotoga neapolitana, glycoside hydrolase family 3
in
Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00
volume
63
issue
9
pages
802 - 806
publisher
Wiley-Blackwell
external identifiers
  • scopus:34548413777
  • wos:000249154300023
ISSN
2053-230X
DOI
10.1107/S1744309107040341
language
English
LU publication?
yes
id
12797f7b-0e6c-45bb-b454-535e2fe43689 (old id 745390)
date added to LUP
2008-01-09 09:58:41
date last changed
2017-01-01 06:46:24
@article{12797f7b-0e6c-45bb-b454-535e2fe43689,
  abstract     = {-Glucosidases belong to families 1, 3 and 9 of the glycoside hydrolases and act on cello-oligosaccharides. Family 1 and 3 enzymes are retaining and are reported to have transglycosylation activity, which can be used to produce oligosaccharides and glycoconjugates. Family 3 enzymes are less well characterized than their family 1 homologues and to date only two crystal structures have been solved. Here, the expression, purification, crystallization and X-ray diffraction data of a family 3 -glucosidase from the hyperthermophilic bacterium Thermotoga neapolitana are reported. Crystals of selenomethionine-substituted protein have also been grown. The crystals belong to space group C2221, with unit-cell parameters a = 74.9, b = 127.0, c = 175.2 Å. Native data have been collected to 2.4 Å resolution and the structure has been solved to 2.7 Å using the selenomethionine MAD method. Model building and refinement of the structure are under way.},
  author       = {Turner, Pernilla and Pramhed, Anna and Kanders, Erik and Hedström, Martin and Nordberg Karlsson, Eva and Logan, Derek},
  issn         = {2053-230X},
  keyword      = {multiple-wavelength anomalous dispersion.,selenomethionine incorporation,Thermotoga neapolitana,glycoside hydrolase family 3},
  language     = {eng},
  number       = {9},
  pages        = {802--806},
  publisher    = {Wiley-Blackwell},
  series       = {Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00},
  title        = {Expression, purification, crystallisation and preliminary X-ray diffraction analysis of Thermotoga neapolitana beta-glucosidase B},
  url          = {http://dx.doi.org/10.1107/S1744309107040341},
  volume       = {63},
  year         = {2007},
}