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Volumn 2013, Issue 2, 2013, Pages

Erratum to Gently does it for submicron crystals (eLife, (2013), 2, (e01662), 10.7554/eLife.01662);Gently does it for submicron crystals

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME; PROTEIN;

EID: 84888081345     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.01979     Document Type: Erratum
Times cited : (4)

References (13)
  • 1
    • 84875766495 scopus 로고    scopus 로고
    • X-ray free electron lasers motivate bioanalytical characterization of protein nanocrystals: Serial femtosecond crystallography
    • doi: 10.1021/ac303716r
    • Bogan MJ. 2013. X-ray free electron lasers motivate bioanalytical characterization of protein nanocrystals: serial femtosecond crystallography. Anal Chem 85:3464-71. doi: 10.1021/ac303716r
    • (2013) Anal Chem , vol.85 , pp. 3464-3471
    • Bogan, M.J.1
  • 2
    • 84864004802 scopus 로고    scopus 로고
    • High-resolution protein structure determination by serial femtosecond crystallography
    • doi: 10.1126/science.1217737
    • Boutet S, Lomb L, Williams GJ, Barends TRM, Aquila A, Doak RB, et al. 2012. High-resolution protein structure determination by serial femtosecond crystallography. Science 337:362-4. doi: 10.1126/science.1217737
    • (2012) Science , vol.337 , pp. 362-364
    • Boutet, S.1    Lomb, L.2    Williams, G.J.3    Barends, T.R.M.4    Aquila, A.5    Doak, R.B.6
  • 3
  • 4
    • 77950813607 scopus 로고    scopus 로고
    • Radiation damage in macromolecular crystallography: What is it and why should we care?
    • doi: 10.1107/S0907444910008656
    • Garman EF. 2010. Radiation damage in macromolecular crystallography: what is it and why should we care? Acta Crystallogr D Biol Crystallogr 66:339-51. doi: 10.1107/S0907444910008656
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 339-351
    • Garman, E.F.1
  • 5
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • doi: 10.1017/S003358350000305X
    • Henderson R. 1995. The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. Q Rev Biophys 28:171-93. doi: 10.1017/S003358350000305X
    • (1995) Q Rev Biophys , vol.28 , pp. 171-193
    • Henderson, R.1
  • 6
    • 77950799462 scopus 로고    scopus 로고
    • The minimum crystal size needed for a complete diffraction data set
    • doi: 10.1107/ S0907444910007262
    • Holton JM, Frankel KA. 2010. The minimum crystal size needed for a complete diffraction data set. Acta Crystallogr D Biol Crystallogr 66:393-408. doi: 10.1107/ S0907444910007262
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 393-408
    • Holton, J.M.1    Frankel, K.A.2
  • 7
    • 75049083128 scopus 로고    scopus 로고
    • How baculovirus polyhedra fit square pegs into round holes to robustly package viruses
    • doi: 10.1038/emboj.2009.352
    • Ji X, Sutton G, Evans G, Axford D, Owen R, Stuart DI. 2010. How baculovirus polyhedra fit square pegs into round holes to robustly package viruses. EMBO J 29:505-14. doi: 10.1038/emboj.2009.352
    • (2010) EMBO J , vol.29 , pp. 505-514
    • Ji, X.1    Sutton, G.2    Evans, G.3    Axford, D.4    Owen, R.5    Stuart, D.I.6
  • 8
    • 84879330227 scopus 로고    scopus 로고
    • A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals
    • doi: 10.1107/S0907444913009700
    • Nederlof I, van Genderen E, Li YW, Abrahams JP. 2013. A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals. Acta Crystallogr D Biol Crystallogr 69:1223-30. doi: 10.1107/S0907444913009700
    • (2013) Acta Crystallogr D Biol Crystallogr , vol.69 , pp. 1223-1230
    • Nederlof, I.1    van Genderen, E.2    Li, Y.W.3    Abrahams, J.P.4
  • 9
    • 0034680144 scopus 로고    scopus 로고
    • Potential for biomolecular imaging with femtosecond X-ray pulses
    • doi: 10.1038/35021099
    • Neutze R, Wouts R, van der Spoel D, Weckert E, Hajdu J. 2000. Potential for biomolecular imaging with femtosecond X-ray pulses. Nature 406:752-7. doi: 10.1038/35021099
    • (2000) Nature , vol.406 , pp. 752-757
    • Neutze, R.1    Wouts, R.2    van der Spoel, D.3    Weckert, E.4    Hajdu, J.5
  • 10
    • 84888123895 scopus 로고    scopus 로고
    • A guide to automation and data handling in protein crystallization
    • In: Chayen NE, editor, La Jolla: International University Line
    • Rupp B. 2007. A guide to automation and data handling in protein crystallization. In: Chayen NE, editor. Protein crystallization strategies for structural genomics. La Jolla: International University Line. p. 9-56.
    • (2007) Protein Crystallization Strategies For Structural Genomics , pp. 9-56
    • Rupp, B.1
  • 11
    • 84888087327 scopus 로고    scopus 로고
    • Three-dimensional electron crystallography of protein microcrystals
    • doi: 10.7554/ eLife.01345
    • Shi D, Nannenga BL, Iadanza MG, Gonen T. 2013. Three-dimensional electron crystallography of protein microcrystals. eLife 2:e01345. doi: 10.7554/ eLife.01345
    • (2013) ELife , vol.2
    • Shi, D.1    Nannenga, B.L.2    Iadanza, M.G.3    Gonen, T.4
  • 12
    • 84855984763 scopus 로고    scopus 로고
    • Structure of HDAC3 bound to co-repressor and inositol tetraphosphate
    • doi: 10.1038/ nature10728
    • Watson PJ, Fairall L, Santos GM, Schwabe JWR. 2012. Structure of HDAC3 bound to co-repressor and inositol tetraphosphate. Nature 481:335-40. doi: 10.1038/ nature10728
    • (2012) Nature , vol.481 , pp. 335-340
    • Watson, P.J.1    Fairall, L.2    Santos, G.M.3    Schwabe, J.W.R.4
  • 13
    • 80054063377 scopus 로고    scopus 로고
    • Advances in structural and functional analysis of membrane proteins by electron crystallography
    • doi: 10.1016/j.str.2011.09.001
    • Wisedchaisri G, Reichow SL, Gonen T. 2011. Advances in structural and functional analysis of membrane proteins by electron crystallography. Structure 19:1381-93. doi: 10.1016/j.str.2011.09.001
    • (2011) Structure , vol.19 , pp. 1381-1393
    • Wisedchaisri, G.1    Reichow, S.L.2    Gonen, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.