Hendrickson Wayne A, Teeter Martha M
Laboratory for the Structure of Matter, Naval Research Laboratory 6030, Washington DC 20375, USA.
Department of Chemistry, Boston University, 685 Commonwealth Avenue, Boston, Massachusetts 02215, USA.
Nature. 1981 Mar 12;290(5802):107-113. doi: 10.1038/290107a0.
The highly ordered crystal structure of crambin has been solved at 1.5 Å resolution directly from the diffraction data of a native crystal at a wavelength remote from the sulphur absorption edge. The molecule has three disulphide bridges among its 46 amino acid residues, of which 46% are in helices and 17% are in a β-sheet. Crambin is shown to be an amphipathic protein, inasmuch as its six charged groups are segregated from hydrophobic surface elements. Phasing methods used here will also apply elsewhere.
已直接从天然晶体在远离硫吸收边缘的波长下的衍射数据中，以1.5埃的分辨率解析出了胰凝乳蛋白酶原的高度有序晶体结构。该分子在其46个氨基酸残基中有三个二硫键，其中46%处于螺旋结构，17%处于β折叠结构。已证明胰凝乳蛋白酶原是一种两亲性蛋白质，因为其六个带电基团与疏水表面元件分隔开。这里使用的相位测定方法也将适用于其他地方。
