HETEROGENEOUS AND EPITAXIAL NUCLEATION OF PROTEIN CRYSTALS ON MINERAL SURFACES
HETEROGENEOUS AND EPITAXIAL NUCLEATION OF PROTEIN CRYSTALS ON MINERAL SURFACES
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DOI：
10.1126/science.239.4838.385
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发表时间：
1988-01-22
期刊：
影响因子：
56.9
通讯作者：
SHLICHTA, P
中科院分区：
文献类型：
--
作者：
MCPHERSON, A;SHLICHTA, P
测试了50种不同的矿物样品作为四种常见结晶蛋白质的潜在异质或外延核。通过传统的蛋白质结晶技术发现，每种蛋白质都有一组矿物底物，这些底物在较低的临界过饱和水平下促进晶体的成核，而不是自发生长所需的。在许多涉及所有四种蛋白质的例子中，观察到晶体习性的改变，在某些情况下，由于矿物成核剂的存在，促进了单位细胞的特性。在溶菌酶在岩石上生长的至少一个例子中，晶格分析和x射线衍射表明，蛋白质晶体在岩石上的成核和生长很可能涉及直接的晶格匹配。
Fifty different mineral samples were tested as potential heterogeneous or epitaxial nucleants for four commonly crystallized proteins. It was found, by conventional protein crystallization techniques, that for each protein there was a set of mineral substrates that promoted nucleation of crystals at lower critical levels of supersaturation than required for spontaneous growth. Numerous examples, involving all four proteins, were observed of modification of crystal habit and, in some cases, unit cell properties promoted by the presence of the mineral nucleants. In at least one case, the growth of lysozyme on the mineral apophyllite, it was shown by lattice analysis and x-ray diffraction that the nucleation and growth of the protein crystal on the mineral was likely to involve a direct lattice match.