LAUE CRYSTALLOGRAPHIC STUDIES OF BIOLOGICAL INTERMEDIATE

描述：这是一个富有想象力的节目的第一个续集 旨在使用捕集方法分离反应中间体的研究， 然后用单色X射线或劳厄研究它们的结构 适当的结晶学。第一个项目期导致了一些 无论是在方法开发方面，还是在 所研究的实际中间体的术语。在这一宝贵的基础上 根据经验，斯托达德博士现在建议朝三个方向发展：(I) 确定裂解锤头状核酶结构的结构，(Ii)至 看看能否及时研究核酶切割反应(III) 确定一类新型内切核酸酶的两个成员的结构， 内含子编码酶CREI和PpoI。在结构确定之后 MIR，然后这些酶将被用于旨在确定 反应中间体的结构。(Iv)斯托达德博士的目标是开发 溶剂捕捉法研究化学不稳定的中间体。 具体地说，他计划研究米氏络合物的反应 超氧阴离子和超氧化物歧化酶。

DESCRIPTION: This is the first continuation of an imaginative program of research aimed at using trapping methods to isolate reaction intermediates, and then study their structures using either monochromatic X-rays or Laue crystallography, as appropriate. The first project period led to a number of successful experiments, both in terms of method development and also in terms of actual intermediates that were studied. Building on this valuable experience, Dr. Stoddard now proposes to move in three directions: (i) to determine the structure of a cleaved hammerhead ribozyme structure, (ii) to see if the ribozyme cleavage reaction can be studied in time (iii) to determine the structures of two members of a novel class of endo nucleases, the intron coded enzymes CreI and PpoI. After structure determination by MIR, these enzymes will then be utilized in studies aimed at determining the structures of reaction intermediates. (iv) Dr. Stoddard aims to develop solvent trapping methods to study chemically labile intermediates. Specifically, he plans to study the reaction of the Michaelis complex of the superoxide anion and superoxide dismutase.