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 Communications
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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/745390
- author
- Turner, Pernilla
LU
; Pramhed, Anna
LU
; Kanders, Erik
; Hedström, Martin
LU
; Nordberg Karlsson, Eva
LU
and Logan, Derek
LU
- organization
- publishing date
- 2007
- 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 Communications
- volume
- 63
- issue
- 9
- pages
- 802 - 806
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:34548413777
- wos:000249154300023
- pmid:17768360
- 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
- 2016-04-01 15:46:42
- date last changed
- 2025-10-14 11:39:33
@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}},
keywords = {{multiple-wavelength anomalous dispersion.; selenomethionine incorporation; Thermotoga neapolitana; glycoside hydrolase family 3}},
language = {{eng}},
number = {{9}},
pages = {{802--806}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Acta Crystallographica. Section F: Structural Biology and Crystallization Communications}},
title = {{Expression, purification, crystallisation and preliminary X-ray diffraction analysis of Thermotoga neapolitana beta-glucosidase B}},
url = {{http://dx.doi.org/10.1107/S1744309107040341}},
doi = {{10.1107/S1744309107040341}},
volume = {{63}},
year = {{2007}},
}