Does anyone have a good reference (beyond the original Crick & Magdoff work) for the magnitude of non-isomorphism typically observed in protein crystals? For example, two crystals from the same drop usually yield scaled intensities that are within ~10% of each other, but cryo-cooling usually changes F by 10-20%. At least, that has always been my "impression", but now I find myself in need of a reference for this. Surely someone has done some kind of survey of R-iso between cryo and RT data sets?

-James Holton
MAD Scientist

Reply via email to