Crystallization and preliminary X-ray diffraction studies of arginase from a thermophilic organism Bacillus caldevelox.Acta Crystallogr D Biol Crystallogr. 1995 Sep 01; 51(Pt 5):840-1.AC
Abstract
A thermostable hexameric arginase purified from the extreme thermophile Bacillus caldevelox has been crystallized from Hepes buffer at pH 7.5 in the presence of 12% polyethylene glycol 4000 and 10% 2-propanol, and from cacodylate buffer at pH 7.2 in the presence of 15% 2-propanol and sodium citrate. The latter crystals are more suitable for X-ray diffraction analysis. The crystals are in the orthorhombic space group P2(1)2(1)2(1) with unit-cell dimensions a = 156.3, b = 148.0 and c = 85.4 A. The asymmetric unit contains one hexamer (approximate molecular mass 183 kDa) and has a solvent content of approximately 54%. The crystals diffract to 2.8 A resolution.
Pub Type(s)
Journal Article
Language
eng
PubMed ID
15299821
Citation
Smith, C A., et al. "Crystallization and Preliminary X-ray Diffraction Studies of Arginase From a Thermophilic Organism Bacillus Caldevelox." Acta Crystallographica. Section D, Biological Crystallography, vol. 51, no. Pt 5, 1995, pp. 840-1.
Smith CA, Pratchett ML, Baker EN. Crystallization and preliminary X-ray diffraction studies of arginase from a thermophilic organism Bacillus caldevelox. Acta Crystallogr D Biol Crystallogr. 1995;51(Pt 5):840-1.
Smith, C. A., Pratchett, M. L., & Baker, E. N. (1995). Crystallization and preliminary X-ray diffraction studies of arginase from a thermophilic organism Bacillus caldevelox. Acta Crystallographica. Section D, Biological Crystallography, 51(Pt 5), 840-1.
Smith CA, Pratchett ML, Baker EN. Crystallization and Preliminary X-ray Diffraction Studies of Arginase From a Thermophilic Organism Bacillus Caldevelox. Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):840-1. PubMed PMID: 15299821.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction studies of arginase from a thermophilic organism Bacillus caldevelox.
AU - Smith,C A,
AU - Pratchett,M L,
AU - Baker,E N,
PY - 1995/9/1/pubmed
PY - 1995/9/1/medline
PY - 1995/9/1/entrez
SP - 840
EP - 1
JF - Acta crystallographica. Section D, Biological crystallography
JO - Acta Crystallogr D Biol Crystallogr
VL - 51
IS - Pt 5
N2 - A thermostable hexameric arginase purified from the extreme thermophile Bacillus caldevelox has been crystallized from Hepes buffer at pH 7.5 in the presence of 12% polyethylene glycol 4000 and 10% 2-propanol, and from cacodylate buffer at pH 7.2 in the presence of 15% 2-propanol and sodium citrate. The latter crystals are more suitable for X-ray diffraction analysis. The crystals are in the orthorhombic space group P2(1)2(1)2(1) with unit-cell dimensions a = 156.3, b = 148.0 and c = 85.4 A. The asymmetric unit contains one hexamer (approximate molecular mass 183 kDa) and has a solvent content of approximately 54%. The crystals diffract to 2.8 A resolution.
SN - 0907-4449
UR - https://www.unboundmedicine.com/medline/citation/15299821/Crystallization_and_preliminary_X_ray_diffraction_studies_of_arginase_from_a_thermophilic_organism_Bacillus_caldevelox_
DB - PRIME
DP - Unbound Medicine
ER -
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