Abstract
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 × 0.7 × 0.6 mm3 within a month. The crystals belong to the trigonal space group P31 (or P32), with unit cell dimensions of a= 147.12 Å and c= 131.08 Å. The asymmetric unit seems to contain six molecules of dimeric aryles‐terase, with corresponding crystal volume per protein mass (VM) of 2.53 Å3/Da and solvent fraction of 51.5% by volume. The crystals diffract to at least 2.2 Å Bragg spacing when exposed to X‐rays from a rotating‐anode source. X‐ray data have been collected to 2.9 Å Bragg spacing from native crystals. © 1993 Wiley‐Liss, Inc.
Original language | English |
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Pages (from-to) | 213-215 |
Number of pages | 3 |
Journal | Proteins: Structure, Function, and Bioinformatics |
Volume | 15 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1993 Feb |
Externally published | Yes |
Keywords
- X‐ray diffraction
- bacterial esterase
- crystals
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology