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Hi Joe, I think you are wasting your time pursueing molrep. Go for some experimental phases. Try a bromide soak or xenon derivatisation. Provided your molrep solution is correct, you don't need a lot of extra phase information. Cheers, Manfred. ******************************************************************** * * * Dr. Manfred S. Weiss * * * * Team Leader * * * * EMBL Hamburg Outstation Fon: +49-40-89902-170 * * c/o DESY, Notkestr. 85 Fax: +49-40-89902-149 * * D-22603 Hamburg Email: [log in to unmask] * * GERMANY Web: www.embl-hamburg.de/~msweiss/ * * * ******************************************************************** On Fri, 6 Jul 2007, Joe Smith wrote: > Hi all, > > We have been trying to solve a structure of protein-protein complexes using > 3.1A data (one of the proteins is of 120kDa whereas the other is of 20kDa). > The structure of smaller protein is known (individually-100% sequence > identity) whereas the bigger protein does not share more than 10% sequence > identity with the similar proteins solved from other sources. > > Due to some problem in getting Seleno-labelled protein, we have also been > trying to use molecular replacement (MR) to solve the structure. We want to > find out the correct position of smaller protein using MR and then plan to > extend the phases to the whole asymmetric unit (we hope it could be done but > not sure). We are more or less sure about the fold of bigger protein and > expect it to be similar to the other known related structures. > In one of the solution obtained using phaser, the map looks really good, but > this solution doesn't provide good packing of the complex inside the unit > cell. Due to low scattering contribution of the smaller protein, we are > unable to refine any possible solutions using REFMAC. > > We welcome any kind of suggestions in this regard. > > Thanking you in advance. > > Joe >