Hi again, Thank you for your reply.
I know that the loop regions are notorious for crystallization however in this case it is yielding the crystals but with lower quality. Does it not due to the quick crystallization, the lattice has no time to form up. Thats why it is happening. Can I not opt for glycerol, or sitting drop method. Sincerely Deb On Thu, 04 Dec 2008 [EMAIL PROTECTED] wrote : >Dear Deb, > >We've seen the detrimental effects of local disorder time and tme again. >So - yes it is very likely that the putative disordered loops >detrimentally affect the quality of your crystals. > >You can try to engineer your protein to be better - it usually takes a >number of internally engineered constructs to get things right (about 10 >per 350aa protein, in my experience). This is different from terminal >truncations - which also can have a huge effect on crystallization. > >You might also try some of the methods summarized here: >http://www.xtals.org/pdfs/rescue_crystals.pdf > > >Cheers, > >Artem > > > > Dear Members, > > > > I am getting crystals of my protein. The secondary structure prediction > > implies that it has N-terminal with high degree of loop regions. I also > > get some mountable crystals yielding weak diffraction pattern(10 A). The > > quality of the crystals can also be assumed from its texture for it has > > tortuous surface. The big crystals are achieved at very high concentration > > in hanging drop method (44mg/ml) whereas the initial hit (small crystals) > > is at lower concentration in sitting drop (~ 5mg/ml). > > > > I have some queries about it. Does the N terminal loop regions are having > > any effect of the crystal quality. Any suggestions of its quality > > improvement are welcome. I will be highly benefited with your generous > > replies. > > > > Sincerely > > Deb > > >
