-----BEGIN PGP SIGNED MESSAGE----- Hash: SHA1 Dear Eswar,
you can not only alter the protein concentration but also the precipitant concentration. If your protein really is soluble before you set up the crystallisation trials, you are bound to find a condition without crystals by lowering the precipitant concentration (provided they are not growing by "salting-in", but in that case, water would be the precipitant in a way...). Once you are there (just before you get crystals) this is a good condition to try micro-seeding. And think about the nature of the protein. Maybe increasing the temperature is more promising than decreasing? You can also use an additive screen. Good luck, Tim On 08/18/2011 10:24 AM, eswar reddy wrote: > Dear All > > > I was working two domain protein and i have an hexagonal > look like crystals from additive screen, now i am facing problem these > crystal are growing in 2 minutes even in cold room even at lower protein > concentration @2mg/ml . and i have an smeary data of 7 Å, and we thinking > one domain might be flexible and other is stable > > is there anyway to increase the crystal packing .... > > Any suggestions are welcome. > > Eswar Reddy > - -- - -- Dr Tim Gruene Institut fuer anorganische Chemie Tammannstr. 4 D-37077 Goettingen GPG Key ID = A46BEE1A -----BEGIN PGP SIGNATURE----- Version: GnuPG v1.4.10 (GNU/Linux) Comment: Using GnuPG with Mozilla - http://enigmail.mozdev.org/ iD8DBQFOTNQgUxlJ7aRr7hoRAsFrAKDc0n+BCdqhzCXiU5rSpDSWHmonDwCglMwX yqb8be8DnnoAO0CVv05oQ9c= =BieH -----END PGP SIGNATURE-----
