Crystallization and crystal manipulation of a steric chaperone in complex with its lipase substrate
Crystallization and crystal manipulation of a steric chaperone in complex with its lipase substrate
Pauwels, Kris; Loris, Remy; Vandenbussche, Guy; Ruysschaert, Jean‐Marie; Wyns, Lode; Van Gelder, Patrick
2005-08-01 00:00:00
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 P3121 (P3221), with unit‐cell parameters a = b = 122.3, c = 98.2 Å. A procedure is presented which improved the diffraction of these crystals from ∼5 to 2.95 Å. For the second crystal form, which belonged to space group C2 with unit‐cell parameters a = 183.0, b = 75.7, c = 116.6 Å, X‐ray data were collected to 1.85 Å.
http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.pngActa Crystallographica Section FWileyhttp://www.deepdyve.com/lp/wiley/crystallization-and-crystal-manipulation-of-a-steric-chaperone-in-xTl4X75LWi
Crystallization and crystal manipulation of a steric chaperone in complex with its lipase substrate
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 P3121 (P3221), with unit‐cell parameters a = b = 122.3, c = 98.2 Å. A procedure is presented which improved the diffraction of these crystals from ∼5 to 2.95 Å. For the second crystal form, which belonged to space group C2 with unit‐cell parameters a = 183.0, b = 75.7, c = 116.6 Å, X‐ray data were collected to 1.85 Å.
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