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Yes!, there is:

the fraction of occupied protein with substance can be calculated: S / 
(S + Km) with S being the concentration of the compound.

So, if S = Km, half of the sites are occupied (it follows from 
Michaelis-Menten theory).

In order to saturate the enzyme for 90,90909 % with the compound:

1) S = 10 x Kd (concentration of S at least 10 times the Kd)
and
2) S > P (total concentration of S must be larger than total 
concentration of protein or "binding sites")

Depending on the solubility of the compound, this is not always 
possible. In such a case, you need to use DMSO and/or add solid compound 
to the protein solution and leave it for quite some time for the 
compound to finally bind to the protein.

- J. -


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
>
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-- 
Dr. Jeroen R. Mesters
Gruppenleiter Strukturelle Neurobiologie und Kristallogenese
Institut für Biochemie, Universität zu Lübeck
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