针对当前固有的数据存储结构和数据读取展示效率难以支撑,大规模建筑信息模型(building information model,BIM)三维数据快速加载与渲染的问题,本文深入研究了模型轻量化和快速渲染技术。针对使用三角化几何描述的BIM,在最大程度保持模...针对当前固有的数据存储结构和数据读取展示效率难以支撑,大规模建筑信息模型(building information model,BIM)三维数据快速加载与渲染的问题,本文深入研究了模型轻量化和快速渲染技术。针对使用三角化几何描述的BIM,在最大程度保持模型外观不变的前提下,采用了Draco格网压缩算法,通过三角网模型的压缩达到数据逻辑结构轻量化的效果;在处理纹理结构复杂的BIM时,保持纹理清晰度的同时,采用CRN_DXT5技术,最大限度地压缩纹理数据;对于在外观相似、大量重复但空间位置不同的BIM构件,采用几何模型+姿态/位置矩阵的实例化的策略,实现相同几何模型的实例化压缩,大幅降低纹理的存储大小,实现BIM三维数据快速加载与渲染。同时,借助SuperMapiDesktop平台对优化前后数据源效率进行了验证,结果表明,经过轻量化处理的BIM浏览效率得到了大幅度提升。展开更多
In recent years, high yield expression of proteins in E. coli has witnessed rapid progress with developments of new methodologies and technologies. An important advancement has been the development of novel recombinan...In recent years, high yield expression of proteins in E. coli has witnessed rapid progress with developments of new methodologies and technologies. An important advancement has been the development of novel recombinant cloning approaches and protocols to express heterologous proteins for Nuclear Magnetic Resonance (NMR) studies and for isotopic enrichment. Isotope labeling in NMR is necessary for rapid acquisition of high dimensional spectra for structural studies. In addition, higher yield of proteins using various solubility and affinity tags has made protein over-expression cost-effective. Taken together, these methods have opened new avenues for structural studies of proteins and their interactions. This article deals with the different techniques that are employed for over-expression of proteins in E. coli and different methods used for isotope labeling of proteins vis-à-vis NMR spectroscopy.展开更多
文摘针对当前固有的数据存储结构和数据读取展示效率难以支撑,大规模建筑信息模型(building information model,BIM)三维数据快速加载与渲染的问题,本文深入研究了模型轻量化和快速渲染技术。针对使用三角化几何描述的BIM,在最大程度保持模型外观不变的前提下,采用了Draco格网压缩算法,通过三角网模型的压缩达到数据逻辑结构轻量化的效果;在处理纹理结构复杂的BIM时,保持纹理清晰度的同时,采用CRN_DXT5技术,最大限度地压缩纹理数据;对于在外观相似、大量重复但空间位置不同的BIM构件,采用几何模型+姿态/位置矩阵的实例化的策略,实现相同几何模型的实例化压缩,大幅降低纹理的存储大小,实现BIM三维数据快速加载与渲染。同时,借助SuperMapiDesktop平台对优化前后数据源效率进行了验证,结果表明,经过轻量化处理的BIM浏览效率得到了大幅度提升。
文摘In recent years, high yield expression of proteins in E. coli has witnessed rapid progress with developments of new methodologies and technologies. An important advancement has been the development of novel recombinant cloning approaches and protocols to express heterologous proteins for Nuclear Magnetic Resonance (NMR) studies and for isotopic enrichment. Isotope labeling in NMR is necessary for rapid acquisition of high dimensional spectra for structural studies. In addition, higher yield of proteins using various solubility and affinity tags has made protein over-expression cost-effective. Taken together, these methods have opened new avenues for structural studies of proteins and their interactions. This article deals with the different techniques that are employed for over-expression of proteins in E. coli and different methods used for isotope labeling of proteins vis-à-vis NMR spectroscopy.
