@article{Perrakis:ba5019,
author = "Perrakis, Anastassis and Harkiolaki, Maria and Wilson, Keith S. and Lamzin, Victor S.",
title = "{{\it ARP}/{\it wARP} and molecular replacement}",
journal = "Acta Crystallographica Section D",
year = "2001",
volume = "57",
number = "10",
pages = "1445--1450",
month = "Oct",
doi = {10.1107/S0907444901014007},
url = {http://dx.doi.org/10.1107/S0907444901014007},
abstract = {The aim of {\it ARP}/{\it wARP} is improved automation of model building and refinement in macromolecular crystallography. Once a molecular-replacement solution has been obtained, it is often tedious to refine and rebuild the initial (search) model. {\it ARP}/{\it wARP} offers three options to automate that task to varying extents: (i) autobuilding of a completely new model based on phases calculated from the molecular-replacement solution, (ii) updating of the initial model by atom addition and deletion to obtain an improved map and (iii) docking of a structure onto a new (or mutated) sequence, followed by rebuilding and refining the side chains in real space. A few examples are presented where {\it ARP}/{\it wARP} made a considerable difference in the speed of structure solution and/or made possible refinement of otherwise difficult or uninterpretable maps. The resolution range allowing complete autobuilding of protein structures is currently 2.0{\AA}, but for map improvement considerable advances over more conventional refinement techniques are evident even at 3.2{\AA} spacing.},
keywords = {ARP/wARP, model building and refinement},
}