Canaves Jaume M, Page Rebecca, Wilson Ian A, Stevens Raymond C
The Joint Center for Structural Genomics, USA.
J Mol Biol. 2004 Dec 3;344(4):977-91. doi: 10.1016/j.jmb.2004.09.076.
Cost and time reduction are two of the driving forces in the development of new strategies for protein crystallization and subsequent structure determination. Here, we report the analysis of the Thermotoga maritima proteome, in which we compare the proteins that were successfully expressed, purified and crystallized versus the rest of the proteome. This set of almost 500 proteins represents one of the largest, internally consistent, protein expression and crystallization datasets available. The analysis shows that individual parameters, such as isoelectric point, sequence length, average hydropathy, low complexity regions (SEG), and combinations of these biophysical properties for crystallized proteins define a distinct subset of the T. maritima proteome. The distribution profiles of the various biophysical properties in the expression/crystallization set are then used to extract rules to improve target selection and improve the efficiency and output of structural genomics, as well as general structural biology efforts.
成本降低和时间缩短是推动蛋白质结晶及后续结构测定新策略发展的两大驱动力。在此，我们报告了对嗜热栖热菌蛋白质组的分析，其中我们比较了成功表达、纯化和结晶的蛋白质与蛋白质组中的其他蛋白质。这组近500种蛋白质代表了现有的最大、内部一致的蛋白质表达和结晶数据集之一。分析表明，诸如等电点、序列长度、平均亲水性、低复杂性区域（SEG）等单个参数，以及这些结晶蛋白质的生物物理特性组合，定义了嗜热栖热菌蛋白质组的一个独特子集。然后利用表达/结晶组中各种生物物理特性的分布概况来提取规则，以改进目标选择，提高结构基因组学以及一般结构生物学研究的效率和产出。
