Lin, consider yourself lucky if you only have one problem...;-)
regarding your question, poor reproducibility is a common problem with membrane
protein crystallography and is most likely caused by different amounts of
lipids copurifying with your protein. If you want to avoid it (may not be
Dear all,
is there any consensus about PEG refinement? I'm currently refining several
structures with a lot of bound PEG molecules. However I'm completely
confused now which ligand description to use. For example, a search in Hic
up database reveals 12 possible descriptions for PEG, 5 of them used
Hi,
I usually pick up the one that fits best the map (there are several PEG monomers in the ccp4 monomer library to choose from). You should bear in mind that PEG's are a mixture of molecules, quite often floppy, so whatever fits best is the best choice.
Good luck,
Boaz
Boaz
DESY, Hamburg location, is seeking a
Scientist for Protein Nanocrystallography (f/m)
DESY is one of the world’s leading centres for the investigation of the
structure of matter. DESY develops, runs and uses accelerators and
detectors for photon science and particle physics.
The Center for
I doubt there is a consensus on this. Your PEG solution is a mixture of
lengths of polymer and normally you can only see a small fraction of the
PEG molecule. PEG400 will be between 8 and 10 ethylene glycols. Bigger
PEGS probably vary more. My experience is that you can often only see
