PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2010 | 57 | 3 |

Tytuł artykułu

Personal remarks on the future of protein crystallography and structural biology

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Protein crystallography, the main experimental method of structural biology, has undergone in the recent past three revolutionary changes leading to its unexpected renaissance. They were connected with (i) the introduction of synchrotron radiation sources for X-ray diffraction experiments, (ii) implementation of Se-Met multiwavelength anomalous diffraction (MAD) for phasing, and (iii) initiation of structural genomics (SG) programs. It can be foreseen that in the next 10-15 years protein crystallography will continue to be in this revolutionary phase. We can expect not only an; avalanche of protein crystal structures from SG centers, but also attacking of more demanding projects, such as the structure of membrane proteins and of very large macromolecular complexes. On the technological front, the introduction of X-ray radiation from free-electron lasers will revolutionize the experimental possibilities, making feasible even the imaging of single molecules and of intact biological cells.

Wydawca

-

Rocznik

Tom

57

Numer

3

Opis fizyczny

p.261-264,ref.

Twórcy

autor
  • Department of Crystallography, Faculty of Chemistry, Adam Mickiewicz University, and Center of Biocrystallographic Research Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland

Bibliografia

  • Ban N, Nissen P, Hansen J, Moore PB, Steitz TA (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289: 905-920. 
  • Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE (2000) The Protein Data Bank. Nucleic Acids Res 28: 235-242. 
  • Bourgeois D, Royant A (2005) Advances in kinetic protein crystallography. Curr Opin Struct Biol 15: 538-547. 
  • Dauter Z, Dauter M, Dodson E (2002) Jolly SAD. Acta Crystallogr D Biol Crystallogr 58: 494-506. 
  • Dauter Z, Jaskolski M, Wlodawer A (2010) Impact of synchrotron radiation on macromolecular crystallography: A personal view. J Synchrotron Radiat 17: 433-444. 
  • Gilski M (2008) Automation and remote synchrotron data collection. Acta Phys Polon A 114: 331-338.
  • Guillot B, Jelsch C, Podjarny A, Lecomte C (2008) Charge-density analysis of a protein structure at subatomic resolution: the human aldose reductase case. Acta Crystallogr D Biol Crystallogr 64: 567-588. 
  • Hajdu J (2000) Single-molecule X-ray diffraction. Curr Opin Struct Biol 10: 569-573. 
  • Hendrickson WA (1991) Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254: 51-58. 
  • International Human Genome Sequencing Consortium (2001) Initial sequencing and analysis of the human genome. Nature 409: 860-921. 
  • Jelsch C, Teeter MM, Lamzin V, Pichon-Pesme V, Blessing RH, Lecomte C (2000) Accurate protein crystallography at ultra-high resolution: Valence electron distribution in crambin. Proc Natl Acad Sci USA 97: 3171-3176. 
  • Karle J (1980) Some developments in anomalous dispersion for the structural investigation of macromolecular systems in biology. Int J Quantum Chem S7: 357-367.
  • Sayre D (2007) Single-particle imaging. In: Evolving Methods for Macromolecular Crystallography. Read RJ, Sussman JL, eds, pp 181-191. Springer, Dordrecht.
  • Schluenzen F, Tocilj A, Zarivach R, Harms J, Gluehmann M, Janell D, Bashan A, Bartels H, Agmon I, Franceschi F, Yonath A (2000) Structure of functionally activated small ribosomal subunit at 3.3 Å resolution. Cell 102: 615-623. 
  • Selmer M, Dunham CM, Murphy FV, Weixlbaumer A, Petry S, Kelley AC, Weir JR, Ramakrishnan V (2006) Structure of the 70S ribosome complexed wit mRNA and tRNA. Science 313: 1935-1942. 
  • Venter JC, Adams MD, Myers EW (2001) The sequence of the human genome. Science 291: 1304-1351. 
  • Wang J, Dauter M, Alkire R, Joachimiak A, Dauter Z (2007) Triclinic lysozyme at 0.65 Å resolution. Acta Crystallogr D Biol Crystallogr 63: 1254-1268. 
  • Wimberly BT, Brodersen DE, Clemons WM Jr, Morgan-Warren RJ, Carter AP, Vonrhein C, Hartsch T, Ramakrishnan V (2000) Structure of the 30S ribosomal subunit. Nature 407: 327-339. 
  • Wlodawer A, Minor W, Dauter Z, Jaskolski M (2008) Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures. FEBS J 275: 1-21. 

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.dl-catalog-520c001d-89ad-44e6-87db-5ee8558d9b16
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.