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Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp. Acta

Bakhtiar, Shahrzad LU ; Vevudova, Jitka; Hatti-Kaul, Rajni LU and Su, Xiao-Dong LU (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)
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Contribution to journal
publication status
published
subject
in
Acta Crystallographica. Section D: Biological Crystallography
volume
59
issue
3
pages
529 - 531
publisher
John Wiley and 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
2007-06-29 15:58:53
date last changed
2018-01-07 08:57:34
@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 and 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},
  volume       = {59},
  year         = {2003},
}