Direct observation of nucleus structure and nucleation pathways in apoferritin crystallization

Direct observation of nucleus structure and nucleation pathways in apoferritin crystallization
复制标题

DOI:
10.1021/ja003039c
复制
发表时间:
2001-02-14
影响因子:
15
通讯作者:
Vekilov, PG
Vekilov, PG
中科院分区:
化学1区
文献类型:
--
作者:
Yau, ST;Vekilov, PG

文献摘要

被引文献

相似文献

在蛋白质脱铁蛋白从其溶液中结晶的过程中,我们利用原子力显微镜(AFM)原位成像了代表核结构的近临界簇中分子的排列,这些簇比晶核大或小。在过饱和度µ/k(B)T为1.1-1.6-2.3的情况下,原子核含有约50-20-10个分子。晶核内的分子排列类似于晶体体内的分子排列。与通常的看法相反,观察到的原子核并不是紧密的分子簇,而是由几个排列在一个或两个单分子层中的4-7个分子组成的杆状平面阵列。类似地,意想不到的核结构可能很常见,特别是对于各向异性分子。因此,核结构应该被认为是一个变量,通过先进的理论处理。
Using atomic force microscopy (AFM) in situ during the crystallization of the protein apoferritin from its solution, we imaged the arrangement of the molecules in near-critical clusters, larger or smaller than the crystal nucleus, that are representative of the nucleus structure. At supersaturations Delta mu /k(B)T of 1.1 - 1.6 - 2.3, the nuclei contain about 50 - 20 - 10 molecules. The molecular arrangement within the nuclei is similar to that in the crystal bulk. Contrary to the general belief, the observed nuclei are not compact molecular clusters, but are planar arrays of several rods of 4-7 molecules set in one or two monomolecular layers. Similarly unexpected nuclei structures might be common, especially for anisotropic molecules. Hence, the nucleus structure should be considered as a variable by advanced theoretical treatments.