Article (Scientific journals)
Crystallization and preliminary X-ray analysis of a xylanase from the psychrophile Pseudoalteromonas haloplanktis
Van Petegem, F.; Collins, T.; Meuwis, Marie-Alice et al.
2002In Acta Crystallographica. Section D, Biological Crystallography, 58 (Part 9), p. 1494-1496
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Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Van Petegem, F.
Collins, T.
Meuwis, Marie-Alice  ;  Université de Liège - ULiège > GIGA-Management : Plate-forme protéomique
Gerday, Charles ;  Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences)
Feller, Georges ;  Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie
Van Beeumen, J.
Language :
English
Title :
Crystallization and preliminary X-ray analysis of a xylanase from the psychrophile Pseudoalteromonas haloplanktis
Publication date :
September 2002
Journal title :
Acta Crystallographica. Section D, Biological Crystallography
ISSN :
0907-4449
eISSN :
1399-0047
Publisher :
Blackwell Munksgaard, Copenhagen, Denmark
Volume :
58
Issue :
Part 9
Pages :
1494-1496
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 26 January 2010

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