Lecomte C, Guillot B, Muzet N, Pichon-Pesme V, Jelsch C
LCM3B, UMR CNRS 7036, Faculté des Sciences et Techniques, Université Henri Poincaré, Nancy 1, BP 239, 54506 Vandoeuvre-lès-Nancy, France.
Cell Mol Life Sci. 2004 Apr;61(7-8):774-82. doi: 10.1007/s00018-003-3405-0.
The constant advances in synchrotron radiation sources and crystallogenesis methods and the impulse of structural genomics projects have brought biocrystallography to a context favorable to subatomic resolution protein and nucleic acid structures. Thus, as soon as such precision can be frequently obtained, the amount of information available in the precise electron density should also be easily and naturally exploited, similarly to the field of small molecule charge density studies. Indeed, the use of a nonspherical model for the atomic electron density in the refinement of subatomic resolution protein structures allows the experimental description of their electrostatic properties. Some methods we have developed and implemented in our multipolar refinement program MoPro for this purpose are presented. Examples of successful applications to several subatomic resolution protein structures, including the 0.66 angstrom resolution human aldose reductase, are described.
同步辐射源和晶体生成方法的不断进步以及结构基因组学项目的推动，使得生物晶体学处于有利于获得亚原子分辨率蛋白质和核酸结构的环境中。因此，一旦能够频繁获得这样的精度，精确电子密度中可用的信息量也应该能够像小分子电荷密度研究领域那样轻松自然地加以利用。实际上，在亚原子分辨率蛋白质结构精修中使用非球形原子电子密度模型，可以对其静电性质进行实验描述。本文介绍了我们为此目的在多极精修程序MoPro中开发和实施的一些方法。还描述了在几个亚原子分辨率蛋白质结构上成功应用的实例，包括分辨率为0.66埃的人醛糖还原酶。
