2.5(top 20%)
impact factor
5.7K(top 5%)
papers
349.3K(top 1%)
citations
143(top 5%)
h-index
2.5(top 20%)
impact factor
5.8K
all documents
374.0K
doc citations
531(top 1%)
g-index
Top Articles
# | Title | Journal | Year | Citations |
---|---|---|---|---|
1 | Coot: model-building tools for molecular graphics | Acta Crystallographica Section D: Biological Crystallography | 2004 | 26,736 |
2 | Features and development of Coot | Acta Crystallographica Section D: Biological Crystallography | 2010 | 22,799 |
3 | PHENIX: a comprehensive Python-based system for macromolecular structure solution | Acta Crystallographica Section D: Biological Crystallography | 2010 | 20,564 |
4 | The CCP4 suite: programs for protein crystallography | Acta Crystallographica Section D: Biological Crystallography | 1994 | 16,158 |
5 | Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination | Acta Crystallographica Section D: Biological Crystallography | 1998 | 14,711 |
6 | Structure validation in chemical crystallography | Acta Crystallographica Section D: Biological Crystallography | 2009 | 14,659 |
7 | XDS | Acta Crystallographica Section D: Biological Crystallography | 2010 | 13,840 |
8 | Refinement of Macromolecular Structures by the Maximum-Likelihood Method | Acta Crystallographica Section D: Biological Crystallography | 1997 | 13,459 |
9 | MolProbity: all-atom structure validation for macromolecular crystallography | Acta Crystallographica Section D: Biological Crystallography | 2010 | 12,318 |
10 | Overview of theCCP4 suite and current developments | Acta Crystallographica Section D: Biological Crystallography | 2011 | 11,098 |
11 | REFMAC5 for the refinement of macromolecular crystal structures | Acta Crystallographica Section D: Biological Crystallography | 2011 | 7,247 |
12 | Towards automated crystallographic structure refinement with phenix.refine | Acta Crystallographica Section D: Biological Crystallography | 2012 | 4,573 |
13 | PRODRG: a tool for high-throughput crystallography of protein–ligand complexes | Acta Crystallographica Section D: Biological Crystallography | 2004 | 4,230 |
14 | Scaling and assessment of data quality | Acta Crystallographica Section D: Biological Crystallography | 2006 | 4,124 |
15 | PHENIX: building new software for automated crystallographic structure determination | Acta Crystallographica Section D: Biological Crystallography | 2002 | 3,979 |
16 | How good are my data and what is the resolution? | Acta Crystallographica Section D: Biological Crystallography | 2013 | 3,739 |
17 | Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions | Acta Crystallographica Section D: Biological Crystallography | 2004 | 3,380 |
18 | Molecular replacement withMOLREP | Acta Crystallographica Section D: Biological Crystallography | 2010 | 3,149 |
19 | Automated MAD and MIR structure solution | Acta Crystallographica Section D: Biological Crystallography | 1999 | 2,855 |
20 | iMOSFLM: a new graphical interface for diffraction-image processing withMOSFLM | Acta Crystallographica Section D: Biological Crystallography | 2011 | 2,633 |
21 | Raster3D Version 2.0. A program for photorealistic molecular graphics | Acta Crystallographica Section D: Biological Crystallography | 1994 | 2,205 |
22 | Integration, scaling, space-group assignment and post-refinement | Acta Crystallographica Section D: Biological Crystallography | 2010 | 2,116 |
23 | The Protein Data Bank | Acta Crystallographica Section D: Biological Crystallography | 2002 | 2,023 |
24 | HKL-3000: the integration of data reduction and structure solution – from diffraction images to an initial model in minutes | Acta Crystallographica Section D: Biological Crystallography | 2006 | 1,822 |
25 | TheBuccaneersoftware for automated model building. 1. Tracing protein chains | Acta Crystallographica Section D: Biological Crystallography | 2006 | 1,725 |
26 | Use of TLS parameters to model anisotropic displacements in macromolecular refinement | Acta Crystallographica Section D: Biological Crystallography | 2001 | 1,563 |
27 | Likelihood-enhanced fast translation functions | Acta Crystallographica Section D: Biological Crystallography | 2005 | 1,560 |
28 | Maximum-likelihood density modification | Acta Crystallographica Section D: Biological Crystallography | 2000 | 1,548 |
29 | Substructure solution withSHELXD | Acta Crystallographica Section D: Biological Crystallography | 2002 | 1,481 |
30 | Solving structures of protein complexes by molecular replacement withPhaser | Acta Crystallographica Section D: Biological Crystallography | 2007 | 1,452 |
31 | Data processing and analysis with theautoPROCtoolbox | Acta Crystallographica Section D: Biological Crystallography | 2011 | 1,361 |
32 | Iterative model building, structure refinement and density modification with thePHENIX AutoBuildwizard | Acta Crystallographica Section D: Biological Crystallography | 2008 | 1,319 |
33 | An introduction to data reduction: space-group determination, scaling and intensity statistics | Acta Crystallographica Section D: Biological Crystallography | 2011 | 1,266 |
34 | REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use | Acta Crystallographica Section D: Biological Crystallography | 2004 | 1,207 |
35 | The finer things in X-ray diffraction data collection | Acta Crystallographica Section D: Biological Crystallography | 1999 | 1,183 |
36 | Optimal description of a protein structure in terms of multiple groups undergoing TLS motion | Acta Crystallographica Section D: Biological Crystallography | 2006 | 1,175 |
37 | Presenting your structures: theCCP4mgmolecular-graphics software | Acta Crystallographica Section D: Biological Crystallography | 2011 | 1,133 |
38 | A graphical user interface to theCCP4 program suite | Acta Crystallographica Section D: Biological Crystallography | 2003 | 1,099 |
39 | Likelihood-enhanced fast rotation functions | Acta Crystallographica Section D: Biological Crystallography | 2004 | 1,074 |
40 | The integration of macromolecular diffraction data | Acta Crystallographica Section D: Biological Crystallography | 2006 | 1,052 |
41 | Experimental phasing with SHELXC/D/E: combining chain tracing with density modification | Acta Crystallographica Section D: Biological Crystallography | 2010 | 1,041 |
42 | electronic Ligand Builder and Optimization Workbench(eLBOW): a tool for ligand coordinate and restraint generation | Acta Crystallographica Section D: Biological Crystallography | 2009 | 1,035 |
43 | Methods used in the structure determination of bovine mitochondrial F1 ATPase | Acta Crystallographica Section D: Biological Crystallography | 1996 | 999 |
44 | Efficient anisotropic refinement of macromolecular structures using FFT | Acta Crystallographica Section D: Biological Crystallography | 1999 | 867 |
45 | Detection, delineation, measurement and display of cavities in macromolecular structures | Acta Crystallographica Section D: Biological Crystallography | 1994 | 864 |
46 | SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model | Acta Crystallographica Section D: Biological Crystallography | 1999 | 804 |
47 | Decision-making in structure solution using Bayesian estimates of map quality: thePHENIX AutoSolwizard | Acta Crystallographica Section D: Biological Crystallography | 2009 | 804 |
48 | Automated refinement of protein models | Acta Crystallographica Section D: Biological Crystallography | 1993 | 786 |
49 | Pushing the boundaries of molecular replacement with maximum likelihood | Acta Crystallographica Section D: Biological Crystallography | 2001 | 728 |
50 | Further additions to MolScript version 1.4, including reading and contouring of electron-density maps | Acta Crystallographica Section D: Biological Crystallography | 1999 | 712 |