• Citer

Crystallization and crystal manipulation of a steric chaperone in complex with its lipase substrate.

par Pauwels, Kris;Loris, Remy;Vandenbussche, Guy ;Ruysschaert, Jean Marie ;Wyns, Lode;Van Gelder, Patrick
Référence Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 61, Pt 8, page (791-795)
Publication Publié, 2005-08

Article révisé par les pairs

• Accès en ligne
• Détails
• Contenu
• Statistiques

Résumé :

Bacterial lipases that are secreted via the type II secretion pathway require a lipase-specific foldase in order to obtain their native and biologically active conformation in the periplasmic space. The lipase-foldase complex from Burkholderia glumae (319 and 333 residues, respectively) was crystallized in two crystal forms. One crystal form belongs to space group P3(1)21 (P3(2)21), with unit-cell parameters a = b = 122.3, c = 98.2 A. A procedure is presented which improved the diffraction of these crystals from approximately 5 to 2.95 A. For the second crystal form, which belonged to space group C2 with unit-cell parameters a = 183.0, b = 75.7, c = 116.6 A, X-ray data were collected to 1.85 A.