The DOI matches its Crossref record.
Integration of macromolecular diffraction data
Abstract
In this chapter the integration of macromolecular diffraction data from two-dimensional area detectors is described. Data integration refers to the process of obtaining estimates of diffracted intensities (and their standard deviations) from the raw images recorded by an X-ray detector. When collecting data, a decision has to be taken about the magnitude of the angular rotation of the crystal during the recording of each image: the rotation per image can be comparable to, or greater than, the angular reflection range of a typical reflection (coarse ϕ slicing), or it can be much less than the reflection width (fine ϕ slicing). The latter approach allows the use of three-dimensional profile fitting and, providing that the detector is relatively noise-free, improves the quality of the resulting data by minimizing the contribution of the X-ray background to the total measured intensity. Methods of integration are described and integration by simple summation and by profile fitting is discussed. Keywords: background; data integration; detector overloads; errors; integration of diffraction data; outliers; overloads; partially recorded reflections; profile fitting; standard profiles; summation integration
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.
Integrity signals
Registry
Cites
Statistics
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.
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
Cited by
Ismaya, W. T., Rozeboom, H. J., Weijn, A., Mes, J. J., Fusetti, F., Wichers, H. J., & Dijkstra, B. W. (2011) · Biochemistry · doi:10.1021/bi200395t · Cited by 872
Targeting C-reactive protein for the treatment of cardiovascular disease.
Pepys, M. B., Hirschfield, G. M., Tennent, G. A., Ruth Gallimore, J., Kahan, M. C., Bellotti, V., Hawkins, P. N., Myers, R. M., Smith, M. D., Polara, A., et al. (2006) · Nature · doi:10.1038/nature04672 · Cited by 672
Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria
Watt, I. N., Montgomery, M. G., Runswick, M. J., Leslie, A. G. W., & Walker, J. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011099107 · Cited by 513
Self-citationA small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment
Hyer, M. L., Milhollen, M. A., Ciavarri, J., Fleming, P., Traore, T., Sappal, D., Huck, J., Shi, J., Gavin, J., Brownell, J., et al. (2018) · Nature Medicine · doi:10.1038/nm.4474 · Cited by 447
The Molecular Basis for the Endocytosis of Small R-SNAREs by the Clathrin Adaptor CALM
Miller, S. E., Sahlender, D. A., Graham, S. C., Höning, S., Robinson, M. S., Peden, A. A., & Owen, D. J. (2011) · Cell · doi:10.1016/j.cell.2011.10.038 · Cited by 192
Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery
Oberoi, J., Fairall, L., Watson, P. J., Yang, J.-C., Czimmerer, Z., Kampmann, T., Goult, B. T., Greenwood, J. A., Gooch, J. T., Kallenberger, B. C., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1983 · Cited by 165
Krajewski, W. W., Collins, R., Holmberg-Schiavone, L., Jones, T. A., Karlberg, T., & Mowbray, S. L. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.029 · Cited by 135
Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein
Healey, E. G., Bishop, B., Elegheert, J., Bell, C. H., Padilla-Parra, S., & Siebold, C. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3016 · Cited by 112
The structure of the KtrAB potassium transporter
Vieira-Pires, R. S., Szollosi, A., & Morais-Cabral, J. H. (2013) · Nature · doi:10.1038/nature12055 · Cited by 109
Garavaglia, S., Bruzzone, S., Cassani, C., Canella, L., Allegrone, G., Sturla, L., Mannino, E., Millo, E., De Flora, A., & Rizzi, M. (2012) · Biochemical Journal · doi:10.1042/bj20111263 · Cited by 94
Recognition of protein-linked glycans as a determinant of peptidase activity
Noach, I., Ficko-Blean, E., Pluvinage, B., Stuart, C., Jenkins, M. L., Brochu, D., Buenbrazo, N., Wakarchuk, W., Burke, J. E., Gilbert, M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615141114 · Cited by 89
The IDOL-UBE2D complex mediates sterol-dependent degradation of the LDL receptor
Zhang, L., Fairall, L., Goult, B. T., Calkin, A. C., Hong, C., Millard, C. J., Tontonoz, P., & Schwabe, J. W. R. (2011) · Genes & Development · doi:10.1101/gad.2056211 · Cited by 86
Assembly and solution structure of the core retromer protein complex
Norwood, S. J., Shaw, D. J., Cowieson, N. P., Owen, D. J., Teasdale, R. D., & Collins, B. M. (2011) · Traffic · doi:10.1111/j.1600-0854.2010.01124.x · Cited by 84
Docquier, J.-D., Benvenuti, M., Calderone, V., Stoczko, M., Menciassi, N., Rossolini, G. M., & Mangani, S. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00409-10 · Cited by 51
Clarke, T. A., Kemp, G. L., Wonderen, J. H. V., Doyle, R.-M. A. S., Cole, J. A., Tovell, N., Cheesman, M. R., Butt, J. N., Richardson, D. J., & Hemmings, A. M. (2008) · Biochemistry · doi:10.1021/bi702175w · Cited by 40
Zhang, W., Zeng, F., Liu, Y., Zhao, Y., Lv, H., Niu, L., Teng, M., & Li, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463901 · Cited by 40
Molecular Architecture of the Ankyrin SOCS Box Family of Cul5-Dependent E3 Ubiquitin Ligases
Muniz, J. R. C., Guo, K., Kershaw, N. J., Ayinampudi, V., von Delft, F., Babon, J. J., & Bullock, A. N. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.06.015 · Cited by 34
Metadata
- Authors
- Leslie, A. G. W.
- Venue
- International Tables for Crystallography
- Published
- 2006-10-01
- Pages
- 212-217
- OpenAlex
- W2913186510
- Cited by
- 696
- References
- 0
- FWCI
- 199.49
- Type
- book chapter
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
