Literature DB >> 15299891

Crystallization and preliminary X-ray diffraction studies of the Pseudomonas marginata esterase EstB.

U G Wagner1, B Sölkner, E I Petersen, A Schlacher, H Schwab, C Kratky.   

Abstract

Crystals of the esterase EstB were obtained at 277 K with the hanging-drop technique from polyethylene glycol 4000 solutions containing 2-propanol at pH 7.5. The crystals belong to the trigonal space group P3(1)21 (or P3(2)21) with cell dimensions a = b = 82.9 and c = 193.4 A (at 100 K). The crystals diffract beyond a resolution of 2.0 A.

Entities:  

Year:  1997        PMID: 15299891     DOI: 10.1107/S0907444997004988

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity.

Authors:  Ulrike G Wagner; Evamaria I Petersen; Helmut Schwab; Christoph Kratky
Journal:  Protein Sci       Date:  2002-03       Impact factor: 6.725

  1 in total

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