Crystallization and preliminary X-ray crystallographic analysis of arylesterase from Pseudomonas fluorescens.

Large crystals of arylesterase from Pseudomonas fluorescens have been grown at room temperature using ammonium sulfate as a precipitant. They grow to dimensions of 0.7 x 0.7 x 0.6 mm3 within a month. The crystals belong to the trigonal space group P3(1) (or P3(2)), with unit cell dimensions of a = 147.12 angstrom and c = 131.08 angstrom. The asymmetric unit seems to contain six molecules of dimeric arylesterase, with corresponding crystal volume per protein mass (V(M)) of 2.53 angstrom3/Da and solvent fraction of 51.5% by volume. The crystals diffract to at least 2.2 angstrom Bragg spacing when exposed to X-rays from a rotating-anode source. X-ray data have been collected to 2.9 angstrom Bragg spacing from native crystals.
Publisher
WILEY-LISS
Issue Date
1993-02
Language
ENG
Keywords

TRIAD FORMS; PROTEINS; LIPASE; ESTERASES; DETECTOR

Citation

PROTEINS-STRUCTURE FUNCTION AND GENETICS, v.15, no.2, pp.213 - 215

ISSN
0887-3585
URI
http://hdl.handle.net/10203/5758
Appears in Collection
NE-Journal Papers(저널논문)
  • Hit : 350
  • Download : 4
  • Cited 0 times in thomson ci
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡClick to seewebofscience_button
⊙ Cited 9 items in WoSClick to see citing articles inrecords_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0