| 1 | Real-space refinement inPHENIXfor cryo-EM and crystallography | Acta Crystallographica Section D: Structural Biology | 2018 | 2,255 |
| 2 | ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps | Acta Crystallographica Section D: Structural Biology | 2018 | 1,310 |
| 3 | DIALS: implementation and evaluation of a new integration package | Acta Crystallographica Section D: Structural Biology | 2018 | 870 |
| 4 | The CCP4 suite: integrative software for macromolecular crystallography | Acta Crystallographica Section D: Structural Biology | 2023 | 573 |
| 5 | New tools for the analysis and validation of cryo-EM maps and atomic models | Acta Crystallographica Section D: Structural Biology | 2018 | 550 |
| 6 | Polder maps: improving OMIT maps by excluding bulk solvent | Acta Crystallographica Section D: Structural Biology | 2017 | 540 |
| 7 | CCP4i2: the new graphical user interface to theCCP4 program suite | Acta Crystallographica Section D: Structural Biology | 2018 | 409 |
| 8 | AceDRG: a stereochemical description generator for ligands | Acta Crystallographica Section D: Structural Biology | 2017 | 309 |
| 9 | CheckMyMetal: a macromolecular metal-binding validation tool | Acta Crystallographica Section D: Structural Biology | 2017 | 257 |
| 10 | Recent developments in theCCP-EMsoftware suite | Acta Crystallographica Section D: Structural Biology | 2017 | 249 |
| 11 | KAMO: towards automated data processing for microcrystals | Acta Crystallographica Section D: Structural Biology | 2018 | 227 |
| 12 | Overview of refinement procedures withinREFMAC5: utilizing data from different sources | Acta Crystallographica Section D: Structural Biology | 2018 | 214 |
| 13 | A pipeline approach to single-particle processing inRELION | Acta Crystallographica Section D: Structural Biology | 2017 | 210 |
| 14 | 2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update | Acta Crystallographica Section D: Structural Biology | 2017 | 201 |
| 15 | Automated map sharpening by maximization of detail and connectivity | Acta Crystallographica Section D: Structural Biology | 2018 | 189 |
| 16 | Cryo-EM single-particle structure refinement and map calculation using
Servalcat | Acta Crystallographica Section D: Structural Biology | 2021 | 186 |
| 17 | ZOO: an automatic data-collection system for high-throughput structure analysis in protein microcrystallography | Acta Crystallographica Section D: Structural Biology | 2019 | 177 |
| 18 | Amyloid structure determination in
RELION
-3.1 | Acta Crystallographica Section D: Structural Biology | 2020 | 177 |
| 19 | An introduction to experimental phasing of macromolecules illustrated bySHELX; new autotracing features | Acta Crystallographica Section D: Structural Biology | 2018 | 174 |
| 20 | Diffraction-geometry refinement in theDIALSframework | Acta Crystallographica Section D: Structural Biology | 2016 | 151 |
| 21 | Improved radiation dose efficiency in solution SAXS using a sheath flow sample environment | Acta Crystallographica Section D: Structural Biology | 2016 | 138 |
| 22 | Scaling diffraction data in the DIALS software package: algorithms and new approaches for multi-crystal scaling | Acta Crystallographica Section D: Structural Biology | 2020 | 116 |
| 23 | EIGER detector: application in macromolecular crystallography | Acta Crystallographica Section D: Structural Biology | 2016 | 102 |
| 24 | Pepsi-SAXS: an adaptive method for rapid and accurate computation of small-angle X-ray scattering profiles | Acta Crystallographica Section D: Structural Biology | 2017 | 101 |
| 25 | Electron diffraction data processing withDIALS | Acta Crystallographica Section D: Structural Biology | 2018 | 96 |
| 26 | Approaches to altering particle distributions in cryo-electron microscopy sample preparation | Acta Crystallographica Section D: Structural Biology | 2018 | 92 |
| 27 | Crystal structures of the selenoprotein glutathione peroxidase 4 in its apo form and in complex with the covalently bound inhibitor ML162 | Acta Crystallographica Section D: Structural Biology | 2021 | 92 |
| 28 | Low-dose fixed-target serial synchrotron crystallography | Acta Crystallographica Section D: Structural Biology | 2017 | 91 |
| 29 | Strategies for sample delivery for femtosecond crystallography | Acta Crystallographica Section D: Structural Biology | 2019 | 89 |
| 30 | In-vacuum long-wavelength macromolecular crystallography | Acta Crystallographica Section D: Structural Biology | 2016 | 86 |
| 31 | Sample delivery for serial crystallography at free-electron lasers and synchrotrons | Acta Crystallographica Section D: Structural Biology | 2019 | 86 |
| 32 | A public database of macromolecular diffraction experiments | Acta Crystallographica Section D: Structural Biology | 2016 | 85 |
| 33 | Structural analysis of glycoproteins: building N-linked glycans withCoot | Acta Crystallographica Section D: Structural Biology | 2018 | 84 |
| 34 | Current approaches for the fitting and refinement of atomic models into cryo-EM maps usingCCP-EM | Acta Crystallographica Section D: Structural Biology | 2018 | 77 |
| 35 | Elucidation of protein function using computational docking and hotspot analysis by ClusPro and FTMap | Acta Crystallographica Section D: Structural Biology | 2022 | 77 |
| 36 | Gentle, fast and effective crystal soaking by acoustic dispensing | Acta Crystallographica Section D: Structural Biology | 2017 | 76 |
| 37 | Fixed target combined with spectral mapping: approaching 100% hit rates for serial crystallography | Acta Crystallographica Section D: Structural Biology | 2016 | 75 |
| 38 | Processing serial crystallography data with CrystFEL: a step-by-step guide | Acta Crystallographica Section D: Structural Biology | 2019 | 73 |
| 39 | Implications of
AlphaFold
2 for crystallographic phasing by molecular replacement | Acta Crystallographica Section D: Structural Biology | 2022 | 73 |
| 40 | In meso in situserial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures | Acta Crystallographica Section D: Structural Biology | 2016 | 71 |
| 41 | Protein structure determination by electron diffraction using a single three-dimensional nanocrystal | Acta Crystallographica Section D: Structural Biology | 2017 | 68 |
| 42 | TheXChemExplorergraphical workflow tool for routine or large-scale protein–ligand structure determination | Acta Crystallographica Section D: Structural Biology | 2017 | 67 |
| 43 | Radiation damage in protein crystallography at X-ray free-electron lasers | Acta Crystallographica Section D: Structural Biology | 2019 | 67 |
| 44 | Automated harvesting and processing of protein crystals through laser photoablation | Acta Crystallographica Section D: Structural Biology | 2016 | 63 |
| 45 | Tools for ligand validation inCoot | Acta Crystallographica Section D: Structural Biology | 2017 | 62 |
| 46 | Distributed computing for macromolecular crystallography | Acta Crystallographica Section D: Structural Biology | 2018 | 62 |
| 47 | Microtubule architecturein vitroand in cells revealed by cryo-electron tomography | Acta Crystallographica Section D: Structural Biology | 2018 | 59 |
| 48 | Crystallography on a chip – without the chip: sheet-on-sheet sandwich | Acta Crystallographica Section D: Structural Biology | 2018 | 59 |
| 49 | Automated refinement of macromolecular structures at low resolution using prior information | Acta Crystallographica Section D: Structural Biology | 2016 | 58 |
| 50 | High-density grids for efficient data collection from multiple crystals | Acta Crystallographica Section D: Structural Biology | 2016 | 56 |