Another good trick is to use drop dilution to suppress nucleation. For
example, instead of mixing 1 uL of protein with 1 uL of well solution,
you can try 1 uL of protein + x uL of water + 1 uL of well solution,
where x = 1-10 uL. This will often result in less nucleation and fewer,
larger crystals. We have also used low concentrations (2-10%) of DMSO,
glycerol, or ethylene glycol to suppress nucleation. Sometimes such
tricks work, sometimes they don't.
Cheers,
_______________________________________
Roger S. Rowlett
Gordon & Dorothy Kline Professor
Department of Chemistry
Colgate University
13 Oak Drive
Hamilton, NY 13346
tel: (315)-228-7245
ofc: (315)-228-7395
fax: (315)-228-7935
email: [email protected]
On 7/5/2012 10:46 AM, Michael Murphy wrote:
If you have found a condition that is yielding crystals, but they are
either too many/too small or do not have a very optimal shape, I have
found varying the drop sizes and/or ratios of protein:precipitant
solutions can make a big difference
On Wed, Jul 4, 2012 at 5:33 AM, REX PALMER <[email protected]
<mailto:[email protected]>> wrote:
Does anyone have any new tips/methods for improving crystal size
once the initial conditions have been established?
Rex Palmer
http://www.bbk.ac.uk/biology/our-staff/emeritus-staff
http://rexpalmer2010.homestead.com
