MAGICSQUASH: iterative multiple domain and multiple space group NCS averaging
David J. Schuller · Acta Crystallographica Section A Foundations of Crystallography · 1996
Recently implemented modules and fearmes in the PROTEIN progrru11 system will be in focus that provide high flexibility in the m•ea of density modification m1d mru1ipulation in real space.Real space techniques have been ru1 important issue in PROTEIN Ji-om its very beginning.Original goals of the '"sem•ch methods" in the field of moleculm replacement have been the corTelation of maps for the exploration of non-crystallographic symmetry (Patterson self rotation).positioning of known moleculm models in unknown structmes (cross rotation.trru1slation) both in Patterson ru1d FoUiier map, location _ru1d refinement of local a;;;:es in Fourier map, calculation of ''meru1 Fmuier maps", ru1d rotated density maps.The widely used density modification techniques like molecular averaging and solvent flattening aiming at phase improvement and interpretability of density maps have required further extension and flexibility of these capabilities.Following the principles of PROTEIN, this has been acchieved by implementing additional modules and features (e.g.simple map algebra incl.rotation and supeqJosition, unit-cell generation from an asymmetric unit, mask calculation by convolution techniques).In this way tools are provided to the u~er he can combine with the already present elements to powerful procedures on the level of PROTEIN's flexible command language.PROTEIN itself has been ported to a variety of platforms and is available for the most prominent Unix systems incl.DEC Alpha, Silicon Graphics, IBM RS/6000, Sun and Hewlett Packard, as well as Open VMS on VAX and AXP,.on particular requestThe Web page !zttp:!!wlVw.biochem.mpg.de/PROTEINIhome.!ztml provides detailed information about the package's capabilities, availability, new features, examples, a mailing list for the user community, etc. PS03.03.10