CoChat
Sign Up
Cited by 29,915

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Features and development of Coot

Emsley, P., Lohkamp, B., Scott, W. G., Cowtan, K.·2010·Acta Crystallographica Section D Biological Crystallography
DOI 10.1107/s0907444910007493PMC PMC2852313
Open this paper in CoChat — free account

Abstract

Coot is a molecular-graphics application for model building and validation of biological macromolecules. The program displays electron-density maps and atomic models and allows model manipulations such as idealization, real-space refinement, manual rotation/translation, rigid-body fitting, ligand search, solvation, mutations, rotamers and Ramachandran idealization. Furthermore, tools are provided for model validation as well as interfaces to external programs for refinement, validation and graphics. The software is designed to be easy to learn for novice users, which is achieved by ensuring that tools for common tasks are `discoverable' through familiar user-interface elements (menus and toolbars) or by intuitive behaviour (mouse controls). Recent developments have focused on providing tools for expert users, with customisable key bindings, extensions and an extensive scripting interface. The software is under rapid development, but has already achieved very widespread use within the crystallographic community. The current state of the software is presented, with a description of the facilities available and of some of the underlying methods employed.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1107/s0907444910007493

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1 Coot architecture, showing the layers of functionality from the user interface down to some of the low-level libraries. The libraries are described in more detail in the main text (§§3.4, 3.5, 4.3 and 4.4).
Figure 1 Coot architecture, showing the layers of functionality from the user interface down to some of the low-level libraries. The libraries are described in more detail in the main text (§§3.4, 3.5, 4.3 and 4.4).CC BY · PubMed Central
Figure 2 The Coot main window. The main display area shows a molecule and electron density. At the top of the window is a menu bar providing access to most of the tools. Commonly used model-manipulation tools are also available through the toolbar on the right. Below the menu bar is an area for user-definable buttons. A status bar is displayed below the three-dimensional canvas.
Figure 2 The Coot main window. The main display area shows a molecule and electron density. At the top of the window is a menu bar providing access to most of the tools. Commonly used model-manipulation tools are also available through the toolbar on the right. Below the menu bar is an area for user-definable buttons. A status bar is displayed below the three-dimensional canvas.CC BY · PubMed Central
Figure 3 Mouse controls: a schematic mouse is shown with the clicked button in grey. Additional keys to be pressed are shown to the left of the mouse. On the right-hand side is a schematic of the mouse control action together with an explanation.
Figure 3 Mouse controls: a schematic mouse is shown with the clicked button in grey. Additional keys to be pressed are shown to the left of the mouse. On the right-hand side is a schematic of the mouse control action together with an explanation.CC BY · PubMed Central
Figure 4 Real-space refinement of a mispositioned residue. The coloured bonds show the original structure. The white bonds show the refined atoms after dragging and refinement. The coloured boxes in the pop-up window indicate how well the new model obeys various geometric restraints. Clicking the ‘Accept’ button will cause the coloured atoms to be moved to the new positions.
Figure 4 Real-space refinement of a mispositioned residue. The coloured bonds show the original structure. The white bonds show the refined atoms after dragging and refinement. The coloured boxes in the pop-up window indicate how well the new model obeys various geometric restraints. Clicking the ‘Accept’ button will cause the coloured atoms to be moved to the new positions.CC BY · PubMed Central
Figure 5 A model with an NCS ghost. The thick bonds represent the atoms in one chain of the protein. The thin bonds represent an NCS-related chain transformed to superpose on the first chain. At the bottom of the screen the atoms coincide; at the top the main chain deviates and a side chain is in a different conformation.
Figure 5 A model with an NCS ghost. The thick bonds represent the atoms in one chain of the protein. The thin bonds represent an NCS-related chain transformed to superpose on the first chain. At the bottom of the screen the atoms coincide; at the top the main chain deviates and a side chain is in a different conformation.CC BY · PubMed Central
Figure 6 Electron density with NCS map for the same model and in the same orientation as the previous figure. The blue density is for the original chain. The magenta contour represents the electron density for the NCS-related chain transformed back onto the original chain and clearly showing the differences.
Figure 6 Electron density with NCS map for the same model and in the same orientation as the previous figure. The blue density is for the original chain. The magenta contour represents the electron density for the NCS-related chain transformed back onto the original chain and clearly showing the differences.CC BY · PubMed Central
Figure 7 A typical validation graph. Bars represent individual residues in a chain, with an indication of quality for the residue being given by both the size and colour of the bar. The plot is interactive, i.e. clicking on a bar takes the user to the corresponding residue.
Figure 7 A typical validation graph. Bars represent individual residues in a chain, with an indication of quality for the residue being given by both the size and colour of the bar. The plot is interactive, i.e. clicking on a bar takes the user to the corresponding residue.CC BY · PubMed Central
Figure 8 Screenshot of a classical Ramachandran plot showing all residues, with the axes defining the ϕ and ψ angles (angles in degrees). Preferred regions are coloured in pink, allowed regions in yellow and the background in grey for disallowed regions. Standard residues are shown as dark blue squares, Pro residues as light blue squares and Gly residues as light blue open triangles. Residues in the disallowed regions are coloured red.
Figure 8 Screenshot of a classical Ramachandran plot showing all residues, with the axes defining the ϕ and ψ angles (angles in degrees). Preferred regions are coloured in pink, allowed regions in yellow and the background in grey for disallowed regions. Standard residues are shown as dark blue squares, Pro residues as light blue squares and Gly residues as light blue open triangles. Residues in the disallowed regions are coloured red.CC BY · PubMed Central
Figure 9 Screenshot of a Kleywegt plot (Kleywegt, 1996 ▶) showing Ramachandran differences between two NCS-related chains by connecting lines (angles in degrees). Labels, colouring and symbols are as in the previous figure. Arrows link NCS-related residues.
Figure 9 Screenshot of a Kleywegt plot (Kleywegt, 1996 ▶) showing Ramachandran differences between two NCS-related chains by connecting lines (angles in degrees). Labels, colouring and symbols are as in the previous figure. Arrows link NCS-related residues.CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 1 references

Research works printed but not linked: 43

  1. Adams, 2002, Acta Cryst. D, 58, 1948, 10.1107/S0907444902016657 · DOI · Paper page
  2. Bernstein, 1977, J. Mol. Biol., 112, 535, 10.1016/S0022-2836(77)80200-3 · DOI
  3. Blanc, 2004, Acta Cryst. D, 60, 2210, 10.1107/S0907444904016427 · DOI
  4. Blundell, 2002, Nature Rev. Drug Discov., 1, 45, 10.1038/nrd706 · DOI
  5. Brünger, A. T. (1992). X-PLOR v.3.1. A System for X-ray Crystallography and NMR. New Haven: Yale University Press.
  6. Cowtan, 2000, Acta Cryst. D, 56, 1612, 10.1107/S0907444900013263 · DOI
  7. Cowtan, 2003, IUCr Comput. Commun. Newsl., 2, 4
  8. Cowtan, 2006, Acta Cryst. D, 62, 1002, 10.1107/S0907444906022116 · DOI
  9. Cowtan, 2010, Acta Cryst. D, 66, 470, 10.1107/S090744490903947X · DOI
  10. Dauter, 2006, Acta Cryst. D, 62, 1, 10.1107/S0907444905034050 · DOI
  11. Davis, 2007, Nucleic Acids Res., 35, W375, 10.1093/nar/gkm216 · DOI
  12. Esnouf, 1997, Acta Cryst. D, 53, 665, 10.1107/S0907444997005829 · DOI
  13. Greer, 1974, J. Mol. Biol., 82, 279, 10.1016/0022-2836(74)90591-9 · DOI
  14. Hooft, 1996, Nature (London), 381, 272, 10.1038/381272a0 · DOI
  15. Jones, 1986, EMBO J., 5, 819, 10.1002/j.1460-2075.1986.tb04287.x · DOI
  16. Jones, 1991, Acta Cryst. A, 47, 110, 10.1107/S0108767390010224 · DOI
  17. Kelsey, 1998, Higher-Order and Symbolic Computation, 11, 7, 10.1023/A:1010051815785 · DOI
  18. Kleywegt, 1996, Acta Cryst. D, 52, 842, 10.1107/S0907444995016477 · DOI
  19. Kleywegt, 2004, Acta Cryst. D, 60, 2240, 10.1107/S0907444904013253 · DOI
  20. Kleywegt, G. J. & Jones, T. A. (1994). Proceedings of the CCP4 Study Weekend. From First Map to Final Model, edited by S. Bailey, R. Hubbard & D. Waller, pp. 59-66. Warrington: Daresbury Laboratory.
  21. Kleywegt, 1996, Structure, 4, 1395, 10.1016/S0969-2126(96)00147-5 · DOI
  22. Krissinel, 2004, Acta Cryst. D, 60, 2256, 10.1107/S0907444904026460 · DOI
  23. Krissinel, 2004, Acta Cryst. D, 60, 2250, 10.1107/S0907444904027167 · DOI
  24. Langer, 2008, Nature Protoc., 3, 1171, 10.1038/nprot.2008.91 · DOI · Paper page
  25. Lorensen, 1987, ACM SIGGRAPH Comput. Graph., 21, 163, 10.1145/37402.37422 · DOI
  26. Lovell, 2003, Proteins, 50, 437, 10.1002/prot.10286 · DOI · Paper page
  27. Lovell, 2000, Proteins, 40, 389, 10.1002/1097-0134(20000815)40:3<389::AID-PROT50>3.0.CO;2-2 · DOI
  28. Merritt, 1997, Methods Enzymol., 277, 505, 10.1016/S0076-6879(97)77028-9 · DOI
  29. Murshudov, 1997, Acta Cryst. D, 53, 240, 10.1107/S0907444996012255 · DOI
  30. Oldfield, 2001, Acta Cryst. D, 57, 696, 10.1107/S0907444901003894 · DOI
  31. Potterton, 2004, Acta Cryst. D, 60, 2288, 10.1107/S0907444904023716 · DOI
  32. Robertson, 2007, Science, 315, 1549, 10.1126/science.1136231 · DOI · Paper page
  33. Robertson, 2008, Acta Cryst. D, 64, 738, 10.1107/S0907444908011578 · DOI
  34. Storoni, 2004, Acta Cryst. D, 60, 432, 10.1107/S0907444903028956 · DOI
  35. Terwilliger, 2006, Acta Cryst. D, 62, 915, 10.1107/S0907444906017161 · DOI
  36. Vagin, 2004, Acta Cryst. D, 60, 2184, 10.1107/S0907444904023510 · DOI
  37. Vonrhein, 2007, Methods Mol. Biol., 364, 215
  38. Wang, 2004, Acta Cryst. D, 60, 1244, 10.1107/S0907444904010674 · DOI
  39. Westbrook, J. D., Yang, H., Feng, Z. & Berman, H. M. (2005). International Tables for Crystallography, Vol. G, edited by S. R. Hall & B. McMahon, pp. 539-543. Heidelberg: Springer. · DOI
  40. Williams, 2005, Curr. Opin. Chem. Biol., 9, 371, 10.1016/j.cbpa.2005.06.007 · DOI
  41. Word, 1999, J. Mol. Biol., 285, 1711, 10.1006/jmbi.1998.2400 · DOI
  42. Word, 1999, J. Mol. Biol., 285, 1735, 10.1006/jmbi.1998.2401 · DOI
  43. Zhang, 1997, Methods Enzymol., 277, 53, 10.1016/S0076-6879(97)77006-X · DOI

Cited by

Sorted by citations

Items 401–477 of 477

Metadata

Authors
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K.
Venue
Acta Crystallographica Section D Biological Crystallography
Publisher
International Union of Crystallography (IUCr)
Published
2010-03-24
Volume
66
Issue
4
Pages
486-501
ISSN
0907-4449
DOI
10.1107/s0907444910007493
PMC
PMC2852313
Cited by
29,915
References
1
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review