Kay,

Go with LiCl as a reservoir solution (not necessarily in the protein drop). It can generate a very low water vapor pressure. It will suck the water out of almost anything. The CRC handbook has all the information although buried deep within it. However, the DNA and polysaccharide diffractionists used to bubble air through LiCl solutions to get just the right humidity in the sample changer. They had a nice chart to match LiCl concentration to humidity, but my 33 year old copy has crumbled into dust.

To keep microbatch plates hydrated a week or two longer, we put them into chambers with ~0.5 M LiCl to match ~40% PEG4000 or ~1.5-2 M LiCl to match ~60-70% ammonium sulfate (~2.4 - 3 M). The newer microbatch plates do have little reservoir chambers just for this purpose. The drawback with ammonium sulfate is that you have ammonia transfer and the risk of pH changes.

Michael

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R. Michael Garavito, Ph.D.
Professor of Biochemistry & Molecular Biology
513 Biochemistry Bldg.
Michigan State University
East Lansing, MI 48824-1319
Office:  (517) 355-9724     Lab:  (517) 353-9125
FAX:  (517) 353-9334        Email:  [EMAIL PROTECTED]
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On 07/04/2008, at 15.46, Kay Diederichs wrote:

Dear all,

a protein which we work on is available in low quantity. The only crystallization screen we set up is completely clear, no precipitate, nothing.

Now we would like to modify the reservoirs of this screen, by adding LiCl or Ammoniumsulfate or ... , with the goal of reducing the vapour pressure, to at least get the protein concentration in the drop into the range where "something happens".

Does anyone have advice as to which salt we should add (to the reservoir only)? AmSO4 is only soluble to 4M, LiCl goes to 10M. But vapour pressure reduction is not the same as molarity.

thanks for any insight,

Kay
--
Kay Diederichs http://strucbio.biologie.uni- konstanz.de email: [EMAIL PROTECTED] Tel +49 7531 88 4049 Fax 3183 Fachbereich Biologie, Universität Konstanz, Box M647, D-78457 Konstanz


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