Haupt H, Baudner S
Behringwerke Forschungslaboratorien, Marburg, Bundesrepublik Deutschland.
Behring Inst Mitt. 1988 Apr(82):104-26.
The presently known possibilities and conditions for achieving the crystallization of Albumin, Transthyretin, Retinol-binding Protein, Ceruloplasmin and beta 2-Glycoprotein I are described with respect to our own experiences. For isolating some proteins the crystallization gives rise to a real purification step. Sometimes degrees of purity near to 98 till 99% will be reached. Furthermore crystalline proteins are very important for the determination of the three-dimensional structure by aid of the X-ray diffraction analysis. For this purpose large single crystals are needed with minimum requirements of 0.4 mm length for all the three dimensions. Additionally the crystals must have a high degree of order on the molecular level and should allow recording of the diffraction pattern out to 3 A resolution. From the five proteins described here the three dimensional molecular structure of Transthyretin and Retinol-binding Protein could be elucidated by using the method of the X-ray diffraction analysis.
结合我们自身的经验,阐述了目前已知的使白蛋白、转甲状腺素蛋白、视黄醇结合蛋白、铜蓝蛋白和β2-糖蛋白I结晶的可能性和条件。对于某些蛋白质的分离而言,结晶会带来真正的纯化步骤。有时纯度能达到接近98%至99%。此外,借助X射线衍射分析,结晶蛋白对于三维结构的测定非常重要。为此,需要尺寸至少为0.4毫米(三维均为此要求)的大单晶。此外,晶体在分子水平上必须具有高度的有序性,并且应能记录分辨率达到3埃的衍射图谱。通过X射线衍射分析方法,已阐明了此处所描述的五种蛋白质中转甲状腺素蛋白和视黄醇结合蛋白的三维分子结构。