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Speak to your local friendly NMR spectroscopist - they should be able to tell you quite quickly how much of your protein is disordered/flexible in solution, from a few relatively quick experiments. With a bit more effort, they can even tell you which residues (!) Also, have you looked at your crystal packing? Can your 'half' protein form a sensible crystal, with contact interfaces in all 3 dimensions? And, is there room for a second domain? Does the estimated solvent content of your crystals (from Matthews in CCP4) correlate with what you can visualise, in terms of 'empty' space around your electron density? Regards, Antony. -- Dr Antony W Oliver Cancer Research UK: DNA Repair Enzymes Group Section of Structural Biology The Institute of Cancer Research 237 Fulham Road LONDON SW3 6JB [EMAIL PROTECTED] 020 7153 5488 -- >>> "shivesh kumar" <[EMAIL PROTECTED]> 10/03/06 7:51 AM >>> Dear all, At present we have 2.4A resolution.the protein is supposed to have two domains separated by a 8-residues linker region with 3 glycines which we have checked with DisEMBL.So,one domain is can be flexible.We have done the mass spectroscopy of the protein solution itself and we are trying to check with the crystals also.There is no tag in the protein.We kept two acetate molecules and 13 water molecules and it has two bound calciums. ThanX in advance. shivesh
