作者的工作分為兩類，第一部份是以Ｘ光結晶學的方法，決定下列九個含有咪唑（imidazole） 的化合物單晶結構，並描述其配位幾何和晶體堆疊。藉此熟悉結晶學的技術，以及重建結構的流程與方法，作為第二部份工作的基礎。第二部份是以Ｘ光結晶學的方法，決定雞母珠凝集素(Agglutinin from Abrus precatorius)的單晶結構，描述其與雞母珠毒素(Abrin-a from Abrus precatorius)結構上的差異，並試圖由此分析兩者作為醣體抑制蛋白（ＲＩＰ）在活性上的差異。在與作用標靶28SRNA的docking模擬實驗結果中，觀察到雞母珠凝集素的PRO199無法如同雞母珠毒素的ASN200一般，和標靶28SRNA的G4323形成氫建，此結果支持前人以突變實驗得出的結論。

In the first part, nine crystal structures of imidazole compounds have been determined by X-ray crystallography. Their coordination geometry and crystal packing are described. This part of work helped the author to be accustomed to crystallography. In the second part, the structure of agglutinin from Abrus precatorius has been determined by X-ray crystallography. The structure and the activity as a ribosome-inactivating protein (RIP) have been compared with abrin-a from Abrus precatorius. With docking study, ASN200 of abrin-a was found to be hydrogen bonded with G4323 of 28SRNA, while corresponding PRO199 of agglutinin is a non-polar residue. This may explain the lower toxicity of agglutinin than abrin-a, despite of similarity in secondary structure and the activity cleft of two RIPs.

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