Title | Crystallization and crystal manipulation of a steric chaperone in complex with its lipase substrate. |
Publication Type | Journal Article |
Year of Publication | 2005 |
Authors | Pauwels, K., R. Loris, G. Vandenbussche, J. Marie Ruysschaert, L. Wyns, and P. Van Gelder |
Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
Volume | 61 |
Issue | Pt 8 |
Pagination | 791-5 |
Date Published | 2005 Aug 1 |
ISSN | 1744-3091 |
Keywords | Bacterial Proteins, Burkholderia, Crystallization, Electrophoresis, Polyacrylamide Gel, Lipase, Molecular Chaperones, X-Ray Diffraction |
Abstract | 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. |
DOI | 10.1107/S1744309105023055 |
Alternate Journal | Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |
PubMed ID | 16511160 |
PubMed Central ID | PMC1952342 |
- Log in to post comments
- Google Scholar
- PubMed
- DOI