Comment Re:One big problem. (Score 1) 83
Not only are most proteins not able to use this method, protein crystallography is still as much an art as a science. The process of forming a protein crystal requires a protein solution that very slowly becomes super-saturated to the point that the protein molecules start to clump together. To be any good for crystallography, that clumping has to be very controlled (slighly negative second virial coefficient.) If the clumping is too rapid or too favorable, the protein will just crash out like a scrambled egg. If its too slow or repulsive you can wait years to get a decent crystal.
As it has been pointed out lysozyme is NOT a good test protein -- its been done way to often and will crystallize in dozens of different conditions. Real interesting proteins are difficult to crystalize and sometimes will crystalize once and cannot be repeated. This has led to high-throughput robotic methods of trying thousands of different crystallization conditions. Investing the time and effort to perfect a single condition with magnetic levitation may only be useful once small crystals can be developed by other methods.
I think that the real benefit of this work will be to expand the use of neutron diffraction. Current neutron sources are far less intense than x-ray sources. So increasing the crystal size can help a lot. Finally, it might seem counterintuitive but sometimes "perfect" crystals are actually bad -- too small of a crystal mosaicity (how disordered a crystal is) can actually make getting good diffraction data difficult. In these cases (which unfortunately I have not experienced) the crystals are actually purposefully deformed in order to get measurable diffraction data.
All that being said, anyone know where I can get a 33 tesla magnet? Besides having fun levitating small amphibians, I have this paramagnetic protein I'd like to make into jewlery. . .
As it has been pointed out lysozyme is NOT a good test protein -- its been done way to often and will crystallize in dozens of different conditions. Real interesting proteins are difficult to crystalize and sometimes will crystalize once and cannot be repeated. This has led to high-throughput robotic methods of trying thousands of different crystallization conditions. Investing the time and effort to perfect a single condition with magnetic levitation may only be useful once small crystals can be developed by other methods.
I think that the real benefit of this work will be to expand the use of neutron diffraction. Current neutron sources are far less intense than x-ray sources. So increasing the crystal size can help a lot. Finally, it might seem counterintuitive but sometimes "perfect" crystals are actually bad -- too small of a crystal mosaicity (how disordered a crystal is) can actually make getting good diffraction data difficult. In these cases (which unfortunately I have not experienced) the crystals are actually purposefully deformed in order to get measurable diffraction data.
All that being said, anyone know where I can get a 33 tesla magnet? Besides having fun levitating small amphibians, I have this paramagnetic protein I'd like to make into jewlery. . .
