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 >
