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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Determining the molecular-packing arrangements on protein crystal faces by atomic force microscopy.
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Determining the molecular-packing arrangements on protein crystal faces by atomic force microscopy.

机译:确定molecular-packing安排蛋白质晶体的脸由原子力显微镜。

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Previous atomic force microscopy (AFM) studies and periodic bond-chain (PBC) analyses of tetragonal lysozyme crystals have suggested that the (110) face consists of chains of molecules related to one another by 43 axes parallel to the crystal face. In this study, high-resolution AFM images of the (110) face were obtained and analyzed in order to verify this prediction. A computer program was employed which constructs the theoretical AFM image corresponding to a specific crystallographic molecular-packing arrangement and AFM tip shape. The packing arrangement and tip shape were varied in order to obtain the maximum possible correlation between experimental and theoretical images. The prediction from PBC analysis of an arrangement involving 43 helices was confirmed in this manner, while the alternate arrangement, consisting of molecules related to one another by 21 axes, was not observed. However, the surface structure was found to differ significantly even from this crystallographic arrangement. The molecules were found to pack slightly closer about what will become the 43 axes within the interior of the crystal, suggesting the occurrence of surface reconstruction or rearrangement on the tetragonal lysozyme (110) face. This study represents a new approach for more precise determination of the molecular-packing arrangements on protein crystal faces employing AFM.
机译:和以前的原子力显微镜(AFM)研究正方的周期性bond-chain (PBC)分析溶菌酶晶体表明(110)面对由相关的分子链另一个由43个轴平行于晶体脸的(110)面获得和分析为了验证这种预测。项目采用构造对应于一个特定的理论AFM图像晶体molecular-packing安排和AFM针尖形状。尖的形状是多种多样的为了获得最大可能的相关性实验和理论的图像。分析涉及43个螺旋线的安排以这种方式被证实,而备用安排,相关分子组成另一个21轴,没有观察到。然而,表面结构被发现即使从这个方面有显著的差异晶体的安排。发现包将要稍微近一些成为了43个轴的内部水晶,表明表面的发生重建或重新排列在正方溶菌酶(110)的脸。更精确的测定方法molecular-packing安排在蛋白质晶体面临着采用AFM。

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