Determination of protein structures - A series of fortunate events

被引:38
作者
Chruszcz, Maksymilian [1 ]
Wlodawer, Alexander [2 ]
Minor, Wladek [1 ]
机构
[1] Univ Virginia, Dept Mol Physiol & Biol Phys, Charlottesville, VA 22903 USA
[2] NCI, Macromol Crystallog Lab, Prot Struct Sect, Frederick, MD 21701 USA
关键词
D O I
10.1529/biophysj.108.131789
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Determination of a macromolecular structure using x-ray diffraction is a multistep process that involves a plethora of techniques involving molecular biology, bioinformatics, and physical sciences. Counterintuitively, the success of any or all individual steps does not guarantee the success of the overall process. This review examines the difficulties presented by each step on the path from a gene to the final publication, together with certain lucky (or unlucky) circumstances that can affect the velocity along that path.
引用
收藏
页码:1 / 9
页数:9
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共 72 条
  • [1] PHENIX:: building new software for automated crystallographic structure determination
    Adams, PD
    Grosse-Kunstleve, RW
    Hung, LW
    Ioerger, TR
    McCoy, AJ
    Moriarty, NW
    Read, RJ
    Sacchettini, JC
    Sauter, NK
    Terwilliger, TC
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2002, 58 : 1948 - 1954
  • [2] Crystal structure of a hyperactive Escherichia coli glycerol kinase mutant Gly230 → Asp obtained using microfluidic crystallization devices
    Anderson, Megan J.
    DeLaBarre, Byron
    Raghunathan, Anu
    Palsson, Bernhard O.
    Brunger, Axel T.
    Quake, Stephen R.
    [J]. BIOCHEMISTRY, 2007, 46 (19) : 5722 - 5731
  • [3] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY
    BAILEY, S
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 : 760 - 763
  • [4] The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    Ban, N
    Nissen, P
    Hansen, J
    Moore, PB
    Steitz, TA
    [J]. SCIENCE, 2000, 289 (5481) : 905 - 920
  • [5] Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus Lon reveals the conformational variability in the active sites of Lon proteases
    Botos, I
    Melnikov, EE
    Cherry, S
    Kozov, S
    Makhovskaya, OV
    Tropea, JE
    Gustchina, A
    Rotanova, TV
    Wlodawer, A
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2005, 351 (01) : 144 - 157
  • [6] Predicting protein disorder and induced folding: From theoretical principles to practical applications
    Bourhis, Jean M.
    Canard, Bruno
    Longhi, Sonia
    [J]. CURRENT PROTEIN & PEPTIDE SCIENCE, 2007, 8 (02) : 135 - 149
  • [7] Crystallography & NMR system:: A new software suite for macromolecular structure determination
    Brunger, AT
    Adams, PD
    Clore, GM
    DeLano, WL
    Gros, P
    Grosse-Kunstleve, RW
    Jiang, JS
    Kuszewski, J
    Nilges, M
    Pannu, NS
    Read, RJ
    Rice, LM
    Simonson, T
    Warren, GL
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 : 905 - 921
  • [8] His-tag impact on structure
    Carson, Mike
    Johnson, David H.
    McDonald, Heather
    Brouillette, Christie
    DeLucas, Lawrence J.
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2007, 63 : 295 - 301
  • [9] QUANTITATIVE-ANALYSIS IN THE CHARACTERIZATION AND OPTIMIZATION OF PROTEIN CRYSTAL-GROWTH
    CARTER, CW
    YIN, YH
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1994, 50 : 572 - 590
  • [10] Development of instrumentation and methods for MAD and structural genomics at the SRS, ESRF, CHESS and Elettra facilities
    Cassetta, A
    Deacon, AM
    Ealick, SE
    Helliwell, JR
    Thompson, AW
    [J]. JOURNAL OF SYNCHROTRON RADIATION, 1999, 6 : 822 - 833