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

• 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

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.