Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4810
Title: Expression, purification, crystallization and preliminary X-ray characterization of the class B acid phosphatase (AphA) from Escherichia coli
Authors: C., Forleo
Benvenuti, Manuela 
V., Calderone
S., Schippa
Docquier, JEAN DENIS
M. C., Thaller
Rossolini, GIAN MARIA
Mangani, Stefano 
Keywords: X-ray; crystal structure; magnesium; phosphatase
Issue Date: 2003
Project: None 
Journal: ACTA CRYSTALLOGRAPHICA. SECTION D, BIOLOGICAL CRYSTALLOGRAPHY
Abstract: 
The class B non-specific acid phosphatase AphA from Escherichia coli has been expressed in E coli and purified following a new protocol. ESI mass spectroscopy shows that the purified enzyme solution contains two polypeptides with molecular weights differing by 185 Da corresponding to two different cleavage sites of the signal peptide from the AphA E. coli precursor. Despite the solution heterogeneity, X-ray quality crystals have been obtained. However, the crystals have a tendency to give polymorphs and to lose long-range order with time while maintaining an intact crystal habit. Crystals have been grown in space groups I222 and C2 with three different unit cells and different asymmetric unit contents. Diffraction data to 1.6 Angstrom resolution have been collected with synchrotron radiation at ESRF and DESY.
Description: 
47946
URI: http://hdl.handle.net/20.500.12779/4810
ISSN: 0907-4449
DOI: 10.1107/S0907444903006826
Appears in Collections:Publications

Show full item record

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.