Reference : Crystallization and preliminary X-ray analysis of a xylanase from the psychrophile Ps...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Crystallization and preliminary X-ray analysis of a xylanase from the psychrophile Pseudoalteromonas haloplanktis
Van Petegem, F. [> > > >]
Collins, T. [> > > >]
Meuwis, Marie-Alice mailto [Université de Liège - ULiège > > GIGA-Management : Plate-forme protéomique >]
Gerday, Charles mailto [Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences) >]
Feller, Georges mailto [Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie >]
Van Beeumen, J. [> > > >]
Acta Crystallographica Section D-Biological Crystallography
Blackwell Munksgaard
Part 9
Yes (verified by ORBi)
[en] The 46 kDa xylanase from the Antarctic microorganism Pseudoalteromonas haloplanktis is an enzyme that efficiently catalyzes reactions at low temperatures. Here, the crystallization of both the native protein and the SeMet-substituted enzyme and data collection from both crystals using synchrotron radiation are described. The native data showed that the crystals diffract to 1.3 Angstrom resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.87, b = 90.51, c = 97.23 Angstrom. SAD data collected at the peak of the selenium absorption edge proved to be sufficient to determine the heavy-atom configuration and to obtain electron density of good quality.

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