A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin

J. B. Cooper; D. A. A. Myles

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A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin

机译：劳厄初步中子衍射的研究的天冬氨酸的蛋白酶endothiapepsin

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Until now, no aspartic proteinase has been subjected to a successful neutron diffraction analysis, owing to the limited size of the crystals. However, the recent development of the neutron Laue technique at ILL and EMBL (Grenoble) has allowed the collection of data to 2.2 A on a complex of endothiapepsin with a transition-state analogue. The objective is to define the positions of the protons at the active site by refinement using the neutron data. In line with work on serine proteinases, where neutron diffraction has provided some of the most definitive data on the catalytic mechanism, it is expected that this work will have a major significance for studies of the aspartic proteinase enzymes.

机译：直到现在,没有天冬氨酸的蛋白酶一个成功的中子衍射分析,由于有限的大小晶体。中子劳厄法在生病和EMBL(格勒诺布尔)2.2允许数据的收集在一个复杂的endothiapepsin过渡态模拟。质子在活性部位的位置使用中子数据细化。丝氨酸蛋白酶,中子衍射提供了一些最明确的催化机理上的数据,它是预计,这项工作将有一个专业天冬氨酸的研究的意义蛋白酶酶。

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来源
《Acta crystallographica.Section D. Biological crystallography》 |2000年第2期|246-248|共3页
作者
J. B. Cooper; D. A. A. Myles;
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作者单位

Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton, SO16 7PX, England;

EMBL Grenoble Outstation, 6 Rue Jules Horowitz, BP 156, 38042, Grenoble, CEDEX 9, France;

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正文语种英语
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Aspartic Acid Proteases; Neutron diffraction; Endothia aspartic proteinaseSerine ProteinaseneutronsRefiningneutron diffraction analysisActive Sitehydrogen ions;

机译：天冬氨酸蛋白酶;中子衍射;Endothia天冬氨酸的proteinaseSerineProteinaseneutronsRefiningneutron衍射analysisActive Sitehydrogen离子;

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A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin

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