Dear Roberto, As indicated by others in reply to you the current best practice in protein crystallography is not a rigid application of such a cut off criterion. This is because there is such a diverse range of crystal qualities. However in chemical crystallography where the data quality from such crystals is more homogeneous such a rule is more often required notably as a guard against 'fast and loose' data collection which may occur (to achieve a very high throughput).
As an Editor myself, whilst usually allowing the authors' chosen resolution cut off, I will insist on the data table saying in a footnote the diffraction resolution where I/sig(I) crosses 2.0 and/or, if relevant, where DeltaAnom/sig(DeltaAnom) crosses 1.0. A remaining possible contentious point with a submitting author is where the title of a paper may claim a diffraction resolution that in fact cannot really be substantiated. Best wishes, Yours sincerely, John On Thu, Mar 3, 2011 at 11:29 AM, Roberto Battistutta <roberto.battistu...@unipd.it> wrote: > Dear all, > I got a reviewer comment that indicate the "need to refine the structures at > an appropriate resolution (I/sigmaI of >3.0), and re-submit the revised > coordinate files to the PDB for validation.". In the manuscript I present > some crystal structures determined by molecular replacement using the same > protein in a different space group as search model. Does anyone know the > origin or the theoretical basis of this "I/sigmaI >3.0" rule for an > appropriate resolution? > Thanks, > Bye, > Roberto. > > > Roberto Battistutta > Associate Professor > Department of Chemistry > University of Padua > via Marzolo 1, 35131 Padova - ITALY > tel. +39.049.8275265/67 > fax. +39.049.8275239 > roberto.battistu...@unipd.it > www.chimica.unipd.it/roberto.battistutta/ > VIMM (Venetian Institute of Molecular Medicine) > via Orus 2, 35129 Padova - ITALY > tel. +39.049.7923236 > fax +39.049.7923250 > www.vimm.it > -- Professor John R Helliwell DSc
