Dear Crystallographers and Biochemists, cross-linking, say with gluteraldehyde, is an oft-used method of demonstrating a protein's oligomeric state in solution. I have a difficulty with this, however: theoretically (and in practice!), one can tune the amount of cross-linker to get what ever result is desired, such that any protein with some exposed lysines can be cross-linked in any oligomeric state. How, then, does one evaluate the power of this evidence? Maybe one should do a gradient of gluteraldehyde concentrations, then plot the deviation of the observed cross-linked oligomerization from a theoretical null hypothesis? Seems like this could be done, but I have never seen this in the literature...
Best, Jacob Keller -- ******************************************* Jacob Pearson Keller Northwestern University Medical Scientist Training Program cel: 773.608.9185 email: j-kell...@northwestern.edu *******************************************
