%0 Journal Article
%T Structure of desheptapeptide (B24-B30) insulin in a new crystal form
%A BAO Sujin
%A ZHANG Jiping
%A CHANG Wenrui
%A LIANG Dongcai
%A <br>包素锦
%A 张季平
%A 常文瑞
%A 梁栋材
%J 中国科学C辑(英文版)
%D 1999
%I Springer
%X The structure of desheptapeptide (B24-B30) insulin (DHPI) in a new crystal form (form B) has been determined and refined to 0.2 nm resolution. The crystals were obtained under the same crystallization condition as previously reported crystal form (form A). The overall structures of the two crystal forms are similar but obvious differences can be observed in crystal packing and local conformation. The crystal structures of the two forms show that the two independent molecules in an asymmetric unit from a DHPI dimer, and the dimer formation buries more than 18.20 and 16.95 nm~2 of solvent accessible surfaces for form A and form B DHPI, respectively, the largest among insulin and insulin analogs ever reported. Close examination at crystal packing shows that the dimer-forming surface of DHPI, namely Surface Ⅱ, is normally present in the association of insulin and insulin analogs in their crystal structures. The results demonstrate that Surface Ⅱ is crucially important for the formation of two crystal form
%K insulin
%K desheptapeptide
%K structure
%K association
%K X-ray crystallography<br>
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=180CF3A72E750F3261A8A60EDC957784&aid=3884DBEAA87359CBD0ED301B1B6663E6&yid=B914830F5B1D1078&vid=ECE8E54D6034F642&iid=38B194292C032A66&sid=866F8A6B640835A7&eid=9F8C5EF901EA1E7E&journal_id=1674-7305&journal_name=ScienceChina.Lifesciences&referenced_num=0&reference_num=0