Diffraction data analysis in the presence of radiation damage

被引:56
作者
Borek, Dominika [1 ]
Cymborowski, Marcin [2 ]
Machius, Mischa [1 ]
Minor, Wladek [2 ]
Otwinowski, Zbyszek [1 ]
机构
[1] Univ Texas SW Med Ctr Dallas, Dallas, TX 75390 USA
[2] Univ Virginia, Charlottesville, VA 22908 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2010年 / 66卷
关键词
PROTEIN CRYSTALS; MACROMOLECULAR CRYSTALS; SYNCHROTRON-RADIATION; STRUCTURAL-CHANGES; DATA REDUCTION; X-RAYS; CRYSTALLOGRAPHY; MOLECULES; SPECIMENS; ERRORS;
D O I
10.1107/S0907444909040177
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
In macromolecular crystallography, the acquisition of a complete set of diffraction intensities typically involves a high cumulative dose of X-ray radiation. In the process of data acquisition, the irradiated crystal lattice undergoes a broad range of chemical and physical changes. These result in the gradual decay of diffraction intensities, accompanied by changes in the macroscopic organization of crystal lattice order and by localized changes in electron density that, owing to complex radiation chemistry, are specific for a particular macromolecule. The decay of diffraction intensities is a well defined physical process that is fully correctable during scaling and merging analysis and therefore, while limiting the amount of diffraction, it has no other impact on phasing procedures. Specific chemical changes, which are variable even between different crystal forms of the same macromolecule, are more difficult to predict, describe and correct in data. Appearing during the process of data collection, they result in gradual changes in structure factors and therefore have profound consequences in phasing procedures. Examples of various combinations of radiation-induced changes are presented and various considerations pertinent to the determination of the best strategies for handling diffraction data analysis in representative situations are discussed.
引用
收藏
页码:426 / 436
页数:11
相关论文
共 49 条
  • [1] Ultrahigh-resolution structure of a BPTI mutant
    Addlagatta, A
    Krzywda, S
    Czapinska, H
    Otlewski, J
    Jaskolski, M
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2001, 57 : 649 - 663
  • [2] [Anonymous], 1977, NEW YORK
  • [3] ARNOTT S, 1966, POLYMER, V7, P157
  • [4] Structural effects of radiation damage and its potential for phasing
    Banumathi, S
    Zwart, PH
    Ramagopal, UA
    Dauter, M
    Dauter, Z
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2004, 60 : 1085 - 1093
  • [5] Blake C. C. F, 1962, S INT AT EN AG VIENN, P183
  • [6] Measurement errors and their consequences in protein crystallography
    Borek, D
    Minor, W
    Otwinowski, Z
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2003, 59 : 2031 - 2038
  • [7] The many faces of radiation-induced changes
    Borek, Dominika
    Ginell, Stephan L.
    Cymborowski, Marcin
    Minor, Wladek
    Otwinowski, Zbyszek
    [J]. JOURNAL OF SYNCHROTRON RADIATION, 2007, 14 : 24 - 33
  • [8] A quantitative approach to data-collection strategies
    Bourenkov, GP
    Popov, AN
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2006, 62 : 58 - 64
  • [9] Structural changes in a cryo-cooled protein crystal owing to radiation damage
    Burmeister, WP
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2000, 56 : 328 - 341
  • [10] Can anomalous signal of sulfur become a tool for solving protein crystal structures?
    Dauter, Z
    Dauter, M
    de La Fortelle, E
    Bricogne, G
    Sheldrick, GM
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1999, 289 (01) : 83 - 92