Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp. Acta
(2003) In Acta Crystallographica. Section D: Biological Crystallography 59(3). p.529-531- Abstract
- A novel calcium-independent serine protease from an alkaliphilic bacterium, Nesterenkonia sp. AL20, has been purified and crystallized at 296 K using sodium formate as the main precipitant. This enzyme is optimally active at pH 10, exhibits high stability towards autolytic digestion and its stability is not affected by the presence of EDTA or detergents. The triangular prism-shaped crystals diffracted X-rays to beyond 1.5 Å at a synchrotron beamline, with space group R3 and unit-cell parameters a = b = 92.26, c = 137.88 Å. A complete data set has been collected to 1.39 Å resolution. The asymmetric unit is estimated and confirmed by self-rotation function calculation to contain two molecules, giving a crystal volume per protein mass (VM) of... (More)
- A novel calcium-independent serine protease from an alkaliphilic bacterium, Nesterenkonia sp. AL20, has been purified and crystallized at 296 K using sodium formate as the main precipitant. This enzyme is optimally active at pH 10, exhibits high stability towards autolytic digestion and its stability is not affected by the presence of EDTA or detergents. The triangular prism-shaped crystals diffracted X-rays to beyond 1.5 Å at a synchrotron beamline, with space group R3 and unit-cell parameters a = b = 92.26, c = 137.88 Å. A complete data set has been collected to 1.39 Å resolution. The asymmetric unit is estimated and confirmed by self-rotation function calculation to contain two molecules, giving a crystal volume per protein mass (VM) of 2.68 Å3 Da-1 and a solvent content of 54%. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/129065
- author
- Bakhtiar, Shahrzad LU ; Vevudova, Jitka ; Hatti-Kaul, Rajni LU and Su, Xiao-Dong LU
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Acta Crystallographica. Section D: Biological Crystallography
- volume
- 59
- issue
- 3
- pages
- 529 - 531
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000181609800021
- pmid:12595716
- scopus:0242585435
- ISSN
- 1399-0047
- DOI
- 10.1107/S0907444902020747
- language
- English
- LU publication?
- yes
- id
- c238e3cd-fee7-4423-9957-22abb966575e (old id 129065)
- date added to LUP
- 2016-04-01 16:00:18
- date last changed
- 2022-01-28 08:38:52
@article{c238e3cd-fee7-4423-9957-22abb966575e, abstract = {{A novel calcium-independent serine protease from an alkaliphilic bacterium, Nesterenkonia sp. AL20, has been purified and crystallized at 296 K using sodium formate as the main precipitant. This enzyme is optimally active at pH 10, exhibits high stability towards autolytic digestion and its stability is not affected by the presence of EDTA or detergents. The triangular prism-shaped crystals diffracted X-rays to beyond 1.5 Å at a synchrotron beamline, with space group R3 and unit-cell parameters a = b = 92.26, c = 137.88 Å. A complete data set has been collected to 1.39 Å resolution. The asymmetric unit is estimated and confirmed by self-rotation function calculation to contain two molecules, giving a crystal volume per protein mass (VM) of 2.68 Å3 Da-1 and a solvent content of 54%.}}, author = {{Bakhtiar, Shahrzad and Vevudova, Jitka and Hatti-Kaul, Rajni and Su, Xiao-Dong}}, issn = {{1399-0047}}, language = {{eng}}, number = {{3}}, pages = {{529--531}}, publisher = {{John Wiley & Sons Inc.}}, series = {{Acta Crystallographica. Section D: Biological Crystallography}}, title = {{Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp. Acta}}, url = {{http://dx.doi.org/10.1107/S0907444902020747}}, doi = {{10.1107/S0907444902020747}}, volume = {{59}}, year = {{2003}}, }