Crystallization and preliminary X-ray analysis of a xylanase from the psychrophile Pseudoalteromonas haloplanktis

peer reviewed 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...

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Bibliographic Details
Published in:Acta Crystallographica Section D Biological Crystallography
Main Authors: Van Petegem, F., Collins, T., Meuwis, Marie-Alice, Gerday, Charles, Feller, Georges, Van Beeumen, J.
Format: Article in Journal/Newspaper
Language:English
Published: Blackwell Munksgaard 2002
Subjects:
Life sciences
Biochemistry
biophysics & molecular biology
Sciences du vivant
Biochimie
biophysique & biologie moléculaire
Antarc*
Antarctic
Online Access:https://orbi.uliege.be/handle/2268/15989
https://doi.org/10.1107/S0907444902011666
Description
Summary:peer reviewed 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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