The Km changes with your reservoir, so predictions are limited. In
general if you have a low Km this is favourable but not a given that
your ligand will be found in the electron density map. As a starting
point try a molar ratio of >3 of the ligand to your protein and you
can go as high as you want (assuming it's soluble and does not cost
you an arm and a leg). 50 fold excess has been used in some cases. And
remember for your cryo-step to include your ligand in sufficient
amounts !
Jürgen
On 1 Dec 2008, at 05:31, yangliuqing wrote:
Hello,everyone,
I have a question for cocrystallization, is there some relationship
between Km value and substrate concentration when making
cocrystallization? How can I know the substrate is enough for binding?
Thank you very much!
liuqing
八卦娱乐包打听，MSN资讯速递帮你忙！ 了解详细！
-
Jürgen Bosch
University of Washington
Dept. of Biochemistry, K-426
1705 NE Pacific Street
Seattle, WA 98195
Box 357742
Phone: +1-206-616-4510
FAX: +1-206-685-7002
Web: http://faculty.washington.edu/jbosch
