Crystallization and preliminary X-ray analysis of a xylanase from the psychrophile Pseudoalteromonas haloplanktis.
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 A 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 A. 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.
Laboratorium voor Eiwitbiochemie en Eiwitengineering, Ghent University, Ledeganckstraat 35, B-9000 Gent, Belgium.
Filip
F
Van Petegem
Tony
T
Collins
Marie Alice
MA
Meuwis
Charles
C
Gerday
Georges
G
Feller
Jozef
J
Van Beeumen
D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D031161:Pseudoalteromonas / Q000201:enzymology*; D043325:Xylan Endo-1,3-beta-Xylosidase; D014995:Xylosidases / Q000737:chemistry*
D014995:Xylosidases; D043325:Xylan Endo-1,3-beta-Xylosidase