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
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DOI：
10.1107/s1744309105023055
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发表时间：
2005-08-01
影响因子：
0.9
通讯作者：
Van Gelder, P
中科院分区：
文献类型：
--
作者：
Pauwels, K;Loris, R;Van Gelder, P
通过II型分泌途径分泌的细菌脂肪酶需要脂肪酶特异性折叠酶以在周质空间中获得其天然和生物活性构象。来自Burkholderia glumae的脂肪酶-折叠酶复合物（分别为319和333个残基）以两种晶体形式结晶。一种晶体属于空间群P3（1）21（P3（2）21），晶胞参数a = B = 122.3，c = 98.2埃。提出了一种改进这些晶体的衍射的方法，从近似5埃到2.95埃。对于第二种晶型，其属于空间群C2，晶胞参数a = 183.0，B = 75.7，c = 116.6埃，X射线数据收集到1.85埃。
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 angstrom. A procedure is presented which improved the diffraction of these crystals from similar to 5 to 2.95 angstrom. For the second crystal form, which belonged to space group C2 with unit-cell parameters a = 183.0, b = 75.7, c = 116.6 angstrom, X-ray data were collected to 1.85 angstrom.