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Volumn 16, Issue 5, 2006, Pages 624-629

Radiation damage in macromolecular cryocrystallography

Author keywords

[No Author keywords available]

Indexed keywords

HELIUM; SCAVENGER;

EID: 33749179561     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2006.08.001     Document Type: Review
Times cited : (130)

References (51)
  • 1
    • 33749166525 scopus 로고    scopus 로고
    • Blake C, Phillips DC: Effects of X-irradiaton on single crystals of myoglobin. In Proceedings of the Symposium on the Biological Effects of Ionising radiation at the Molecular Level, Vienna 1962: 183-191.
  • 2
    • 20644441110 scopus 로고    scopus 로고
    • Towards an understanding of radiation damage in cryocooled macromolecular crystals
    • Nave C., and Garman E.F. Towards an understanding of radiation damage in cryocooled macromolecular crystals. J Synchrotron Radiation 12 (2005) 257-260
    • (2005) J Synchrotron Radiation , vol.12 , pp. 257-260
    • Nave, C.1    Garman, E.F.2
  • 3
    • 0034055545 scopus 로고    scopus 로고
    • Structural changes in a cryo-cooled protein crystals owing to radiation damage
    • Burmeister W.P. Structural changes in a cryo-cooled protein crystals owing to radiation damage. Acta Cryst D56 (2000) 328-341
    • (2000) Acta Cryst , vol.D56 , pp. 328-341
    • Burmeister, W.P.1
  • 4
    • 0034654346 scopus 로고    scopus 로고
    • The 'fingerprint' that X-rays can leave on structures
    • Ravelli R.B.G., and McSweeney S.M. The 'fingerprint' that X-rays can leave on structures. Structure Fold Des 8 (2000) 315-328
    • (2000) Structure Fold Des , vol.8 , pp. 315-328
    • Ravelli, R.B.G.1    McSweeney, S.M.2
  • 6
    • 4444294012 scopus 로고    scopus 로고
    • Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction
    • Adam V., Royant A., Niviere V., Molina-Heredia F.P., and Bourgeois D. Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction. Structure 12 (2004) 1729-1740
    • (2004) Structure , vol.12 , pp. 1729-1740
    • Adam, V.1    Royant, A.2    Niviere, V.3    Molina-Heredia, F.P.4    Bourgeois, D.5
  • 7
    • 11244354296 scopus 로고    scopus 로고
    • Specific radiation damage illustrates light-induced structural changes in the photosynthetic reaction center
    • Baxter R.H., Seagle B.L., Ponomarenko N., and Norris J.R. Specific radiation damage illustrates light-induced structural changes in the photosynthetic reaction center. J Am Chem Soc 126 (2004) 16728-16729
    • (2004) J Am Chem Soc , vol.126 , pp. 16728-16729
    • Baxter, R.H.1    Seagle, B.L.2    Ponomarenko, N.3    Norris, J.R.4
  • 8
    • 2942556712 scopus 로고    scopus 로고
    • Crystal structure of nickel-containing superoxide dismutase reveals another type of active site
    • Wuerges J., Lee J.W., Yim Y.I., Yim H.S., Kang S.O., and Carugo K.D. Crystal structure of nickel-containing superoxide dismutase reveals another type of active site. Proc Natl Acad Sci USA 101 (2004) 8569-8574
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8569-8574
    • Wuerges, J.1    Lee, J.W.2    Yim, Y.I.3    Yim, H.S.4    Kang, S.O.5    Carugo, K.D.6
  • 9
    • 24744444728 scopus 로고    scopus 로고
    • 4Ca complex in single crystals of photosystem II: a case study for metalloprotein crystallography
    • An interesting and comprehensive paper on radiation damage at low dose studied by X-ray absorption spectroscopy, which provides evidence for modification of the metal-site structure in photosystem II.
    • 4Ca complex in single crystals of photosystem II: a case study for metalloprotein crystallography. Proc Natl Acad Sci USA 102 (2005) 12047-12052. An interesting and comprehensive paper on radiation damage at low dose studied by X-ray absorption spectroscopy, which provides evidence for modification of the metal-site structure in photosystem II.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12047-12052
    • Yano, J.1    Kern, J.2    Irrgang, K.-D.3    Latimer, M.J.4    Bergmann, U.5    Glatzel, P.6    Pushkar, Y.7    Biesiadka, J.8    Loll, B.9    Sauer, K.10
  • 10
    • 0344950364 scopus 로고    scopus 로고
    • Heat transfer from protein crystals: implications for flash-cooling and X-ray beam heating
    • A careful theoretical analysis of the crystal-beam-solvent heat transfer and the implications for the design of rational cryoprotocols.
    • Kriminski S., Kazmierczak M., and Thorne R.E. Heat transfer from protein crystals: implications for flash-cooling and X-ray beam heating. Acta Cryst D59 (2003) 697-708. A careful theoretical analysis of the crystal-beam-solvent heat transfer and the implications for the design of rational cryoprotocols.
    • (2003) Acta Cryst , vol.D59 , pp. 697-708
    • Kriminski, S.1    Kazmierczak, M.2    Thorne, R.E.3
  • 11
    • 20644462974 scopus 로고    scopus 로고
    • Three-dimensional numerical analysis of convection and conduction cooling of spherical biocrystals with localised heating from synchrotron X-ray beams
    • Thorough theoretical analysis of heat production and transfer during X-ray irradiation, with an excellent discussion of all the variables involved.
    • Mhaisekar A., Kazmierczak M., and Banerjee R. Three-dimensional numerical analysis of convection and conduction cooling of spherical biocrystals with localised heating from synchrotron X-ray beams. J Synchrotron Radiation 12 (2005) 318-328. Thorough theoretical analysis of heat production and transfer during X-ray irradiation, with an excellent discussion of all the variables involved.
    • (2005) J Synchrotron Radiation , vol.12 , pp. 318-328
    • Mhaisekar, A.1    Kazmierczak, M.2    Banerjee, R.3
  • 13
    • 0036849851 scopus 로고    scopus 로고
    • Unit-cell volume change as a metric of radiation damage in crystals of macromolecules
    • Ravelli R.B.G., Theveneau P., McSweeney S., and Caffrey M. Unit-cell volume change as a metric of radiation damage in crystals of macromolecules. J Synchrotron Radiation 9 (2002) 355-360
    • (2002) J Synchrotron Radiation , vol.9 , pp. 355-360
    • Ravelli, R.B.G.1    Theveneau, P.2    McSweeney, S.3    Caffrey, M.4
  • 14
    • 0037227747 scopus 로고    scopus 로고
    • How does radiation damage in protein crystals depend on X-ray dose?
    • Sliz P., Harrison S.C., and Rosenbaum G. How does radiation damage in protein crystals depend on X-ray dose?. Structure 11 (2003) 13-19
    • (2003) Structure , vol.11 , pp. 13-19
    • Sliz, P.1    Harrison, S.C.2    Rosenbaum, G.3
  • 15
    • 33644870851 scopus 로고    scopus 로고
    • Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection?
    • Leiros H.K., Timmins J., Ravelli R.B.G., and McSweeney S.M. Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection?. Acta Cryst D62 (2006) 125-132
    • (2006) Acta Cryst , vol.D62 , pp. 125-132
    • Leiros, H.K.1    Timmins, J.2    Ravelli, R.B.G.3    McSweeney, S.M.4
  • 16
    • 33645498518 scopus 로고    scopus 로고
    • Experimental determination of the radiation dose limit for cryocooled protein crystals
    • Measurement of the experimental dose limit for cryocooled (100 K) protein crystals.
    • Owen R.L., Rudino-Pinera E., and Garman E.F. Experimental determination of the radiation dose limit for cryocooled protein crystals. Proc Natl Acad Sci USA 103 (2006) 4912-4917. Measurement of the experimental dose limit for cryocooled (100 K) protein crystals.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4912-4917
    • Owen, R.L.1    Rudino-Pinera, E.2    Garman, E.F.3
  • 17
    • 4043099008 scopus 로고    scopus 로고
    • X-ray absorption by macromolecular crystals: the effects of wavelength and crystal composition on absorbed dose
    • Murray J.W., Garman E.F., and Ravelli R.B.G. X-ray absorption by macromolecular crystals: the effects of wavelength and crystal composition on absorbed dose. J Applied Crystallography 37 (2004) 513-522
    • (2004) J Applied Crystallography , vol.37 , pp. 513-522
    • Murray, J.W.1    Garman, E.F.2    Ravelli, R.B.G.3
  • 18
    • 0025071357 scopus 로고
    • Cryoprotection of protein crystals against radiation damage in electron and X-ray diffraction
    • Henderson R. Cryoprotection of protein crystals against radiation damage in electron and X-ray diffraction. Proc R Soc Lond B241 (1990) 6-8
    • (1990) Proc R Soc Lond , vol.B241 , pp. 6-8
    • Henderson, R.1
  • 19
    • 20644465999 scopus 로고    scopus 로고
    • On the influence of the incident photon energy on the radiation damage in crystalline biological samples
    • First systematic experimental study to investigate the question: 'is radiation damage in MX wavelength dependent?'
    • Weiss M.S., Panjikar S., Mueller-Dieckmann C., and Tucker P.A. On the influence of the incident photon energy on the radiation damage in crystalline biological samples. J Synchrotron Radiation 12 (2005) 304-309. First systematic experimental study to investigate the question: 'is radiation damage in MX wavelength dependent?'
    • (2005) J Synchrotron Radiation , vol.12 , pp. 304-309
    • Weiss, M.S.1    Panjikar, S.2    Mueller-Dieckmann, C.3    Tucker, P.A.4
  • 20
    • 20644436026 scopus 로고    scopus 로고
    • Will reduced radiation damage occur with very small crystals?
    • Original Monte Carlo simulation that gives hope for collecting MX data from microcrystals.
    • Nave C., and Hill M.A. Will reduced radiation damage occur with very small crystals?. J Synchrotron Radiation 12 (2005) 299-303. Original Monte Carlo simulation that gives hope for collecting MX data from microcrystals.
    • (2005) J Synchrotron Radiation , vol.12 , pp. 299-303
    • Nave, C.1    Hill, M.A.2
  • 21
    • 0036850047 scopus 로고    scopus 로고
    • Investigation of possible free-radical scavengers and metrics for radiation damage in protein cryocrystallography
    • Murray J., and Garman E. Investigation of possible free-radical scavengers and metrics for radiation damage in protein cryocrystallography. J Synchrotron Radiation 9 (2002) 347-354
    • (2002) J Synchrotron Radiation , vol.9 , pp. 347-354
    • Murray, J.1    Garman, E.2
  • 22
    • 21644454831 scopus 로고    scopus 로고
    • Radiation-damage-induced phasing with anomalous scattering: substructure solution and phasing
    • Zwart P.H., Banumathi S., Dauter M., and Dauter Z. Radiation-damage-induced phasing with anomalous scattering: substructure solution and phasing. Acta Cryst D60 (2004) 1958-1963
    • (2004) Acta Cryst , vol.D60 , pp. 1958-1963
    • Zwart, P.H.1    Banumathi, S.2    Dauter, M.3    Dauter, Z.4
  • 24
    • 0042568890 scopus 로고    scopus 로고
    • SAD phasing with triiodide, softer X-rays and some help from radiation damage
    • Evans G., Polentarutti M., Djinovic Carugo K., and Bricogne G. SAD phasing with triiodide, softer X-rays and some help from radiation damage. Acta Cryst D59 (2003) 1429-1434
    • (2003) Acta Cryst , vol.D59 , pp. 1429-1434
    • Evans, G.1    Polentarutti, M.2    Djinovic Carugo, K.3    Bricogne, G.4
  • 25
    • 32944455892 scopus 로고    scopus 로고
    • Radiation-induced site-specific damage of mercury derivatives: phasing and implications
    • Careful and clearly presented analysis of the radiation-induced site-specific damage of mercury derivatives during the phasing of a protein of unknown structure.
    • Ramagopal U.A., Dauter Z., Thirumuruhan R., Fedorov E., and Almo S.C. Radiation-induced site-specific damage of mercury derivatives: phasing and implications. Acta Cryst D61 (2005) 1289-1298. Careful and clearly presented analysis of the radiation-induced site-specific damage of mercury derivatives during the phasing of a protein of unknown structure.
    • (2005) Acta Cryst , vol.D61 , pp. 1289-1298
    • Ramagopal, U.A.1    Dauter, Z.2    Thirumuruhan, R.3    Fedorov, E.4    Almo, S.C.5
  • 27
    • 0344961810 scopus 로고    scopus 로고
    • Low-temperature behavior of water confined by biological macromolecules and its relation to protein dynamics
    • A review summarising previous landmark results on the glass transition in protein crystals, largely by the same author.
    • Weik M. Low-temperature behavior of water confined by biological macromolecules and its relation to protein dynamics. Eur Phys J E Soft Matter 12 (2003) 153-158. A review summarising previous landmark results on the glass transition in protein crystals, largely by the same author.
    • (2003) Eur Phys J E Soft Matter , vol.12 , pp. 153-158
    • Weik, M.1
  • 29
    • 0346366810 scopus 로고    scopus 로고
    • Crystal Structure of the L intermediate of bacteriorhodopsin: evidence for the vertical translocation during the proton pumping cycle
    • One of a series of studies that investigate the light cycle of bacteriorhodopsin while carefully accounting for X-ray radiation-damage, using a cleverly devised experimental protocol.
    • Kouyama T., Nishikawa T., Tokuhisa T., and Okumura H. Crystal Structure of the L intermediate of bacteriorhodopsin: evidence for the vertical translocation during the proton pumping cycle. J Mol Biol 335 2 (2004) 531-546. One of a series of studies that investigate the light cycle of bacteriorhodopsin while carefully accounting for X-ray radiation-damage, using a cleverly devised experimental protocol.
    • (2004) J Mol Biol , vol.335 , Issue.2 , pp. 531-546
    • Kouyama, T.1    Nishikawa, T.2    Tokuhisa, T.3    Okumura, H.4
  • 30
    • 2942752112 scopus 로고    scopus 로고
    • Initial events in the photocycle of photoactive yellow protein
    • Kort R., Hellingwerf K.J., and Ravelli R.B.G. Initial events in the photocycle of photoactive yellow protein. J Biol Chem 279 (2004) 26417-26424
    • (2004) J Biol Chem , vol.279 , pp. 26417-26424
    • Kort, R.1    Hellingwerf, K.J.2    Ravelli, R.B.G.3
  • 31
    • 10044255851 scopus 로고    scopus 로고
    • DNA apophotolyase from Anacystis nidulans: 1.8 Å structure, 8-HDF reconstitution and X-ray-induced FAD reduction
    • Kort R., Komori H., Adachi S., Miki K., and Aker E. DNA apophotolyase from Anacystis nidulans: 1.8 Å structure, 8-HDF reconstitution and X-ray-induced FAD reduction. Acta Cryst D60 (2004) 1205-1213
    • (2004) Acta Cryst , vol.D60 , pp. 1205-1213
    • Kort, R.1    Komori, H.2    Adachi, S.3    Miki, K.4    Aker, E.5
  • 32
    • 0037161809 scopus 로고    scopus 로고
    • The catalytic pathway of horseradish peroxidase at high resolution
    • Ingenious data collection strategy that allowed the observation of snapshots of an X-ray redox titration.
    • Berglund G.I., Carlsson G.H., Smith A.T., Szoke H., Henriksen A., and Hajdu J. The catalytic pathway of horseradish peroxidase at high resolution. Nature 417 (2002) 463-468. Ingenious data collection strategy that allowed the observation of snapshots of an X-ray redox titration.
    • (2002) Nature , vol.417 , pp. 463-468
    • Berglund, G.I.1    Carlsson, G.H.2    Smith, A.T.3    Szoke, H.4    Henriksen, A.5    Hajdu, J.6
  • 33
    • 22444440389 scopus 로고    scopus 로고
    • Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage
    • Dubnovitsky A.P., Ravelli R.B.G., Popov A.N., and Papageorgiou A.C. Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage. Protein Sci 14 (2005) 1498-1507
    • (2005) Protein Sci , vol.14 , pp. 1498-1507
    • Dubnovitsky, A.P.1    Ravelli, R.B.G.2    Popov, A.N.3    Papageorgiou, A.C.4
  • 34
    • 0037830694 scopus 로고    scopus 로고
    • Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function
    • Alphey M.S., Gabrielsen M., Micossi E., Leonard G.A., McSweeney S.M., Ravelli R.B.G., Tetaud E., Fairlamb A.H., Bond C.S., and Hunter W.N. Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function. J Biol Chem 278 (2003) 25919-25925
    • (2003) J Biol Chem , vol.278 , pp. 25919-25925
    • Alphey, M.S.1    Gabrielsen, M.2    Micossi, E.3    Leonard, G.A.4    McSweeney, S.M.5    Ravelli, R.B.G.6    Tetaud, E.7    Fairlamb, A.H.8    Bond, C.S.9    Hunter, W.N.10
  • 35
    • 24344492710 scopus 로고    scopus 로고
    • Oxidised and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF
    • Roberts B.R., Wood Z.A., Jonsson T.J., Poole L.B., and Karplus P.A. Oxidised and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF. Protein Sci 14 (2005) 2414-2420
    • (2005) Protein Sci , vol.14 , pp. 2414-2420
    • Roberts, B.R.1    Wood, Z.A.2    Jonsson, T.J.3    Poole, L.B.4    Karplus, P.A.5
  • 36
    • 10044280323 scopus 로고    scopus 로고
    • Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair
    • Fascinating and well-described structure of a synthetic lesion in DNA, repaired by radiation damage in the X-ray beam.
    • Mees A., Klar T., Gnau P., Hennecke U., Eker A.P.M., Carell T., and Essen L.-O. Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair. Science 306 (2004) 1789-1793. Fascinating and well-described structure of a synthetic lesion in DNA, repaired by radiation damage in the X-ray beam.
    • (2004) Science , vol.306 , pp. 1789-1793
    • Mees, A.1    Klar, T.2    Gnau, P.3    Hennecke, U.4    Eker, A.P.M.5    Carell, T.6    Essen, L.-O.7
  • 37
    • 33644876080 scopus 로고    scopus 로고
    • Some aspects of quantitative analysis and correction of radiation damage
    • Diederichs K. Some aspects of quantitative analysis and correction of radiation damage. Acta Cryst D62 (2006) 96-101
    • (2006) Acta Cryst , vol.D62 , pp. 96-101
    • Diederichs, K.1
  • 38
    • 0038521325 scopus 로고    scopus 로고
    • Zero-dose extrapolation as part of macromolecular synchrotron data reduction
    • Diederichs K., McSweeney S., and Ravelli R.B.G. Zero-dose extrapolation as part of macromolecular synchrotron data reduction. Acta Cryst D59 (2003) 903-909
    • (2003) Acta Cryst , vol.D59 , pp. 903-909
    • Diederichs, K.1    McSweeney, S.2    Ravelli, R.B.G.3
  • 39
    • 16644367850 scopus 로고    scopus 로고
    • Structural effects of radiation damage and its potential for phasing
    • Banumathi S., Zwart P.H., Ramagopal U.A., Dauter M., and Dauter Z. Structural effects of radiation damage and its potential for phasing. Acta Cryst D60 (2004) 1085-1093
    • (2004) Acta Cryst , vol.D60 , pp. 1085-1093
    • Banumathi, S.1    Zwart, P.H.2    Ramagopal, U.A.3    Dauter, M.4    Dauter, Z.5
  • 41
    • 16644393616 scopus 로고    scopus 로고
    • Phasing in the presence of severe site-specific radiation damage through dose-dependent modelling of heavy atoms
    • Adaptation of the widely used phasing program 'Sharp' to account for radiation-damage-induced changes in real space. The authors demonstrate that this can result in greatly improved experimental maps for a brominated RNA structure.
    • Schiltz M., Dumas P., Ennifar E., Flensburg C., Paciorek W., Vonrhein C., and Bricogne G. Phasing in the presence of severe site-specific radiation damage through dose-dependent modelling of heavy atoms. Acta Cryst D60 (2004) 1024-1031. Adaptation of the widely used phasing program 'Sharp' to account for radiation-damage-induced changes in real space. The authors demonstrate that this can result in greatly improved experimental maps for a brominated RNA structure.
    • (2004) Acta Cryst , vol.D60 , pp. 1024-1031
    • Schiltz, M.1    Dumas, P.2    Ennifar, E.3    Flensburg, C.4    Paciorek, W.5    Vonrhein, C.6    Bricogne, G.7
  • 43
    • 33644878458 scopus 로고    scopus 로고
    • A quantitative approach to data collection strategies
    • Statistical modelling of all parameters in the diffraction experiment, including radiation damage, allowing rational optimization of data collection strategies.
    • Bourenkov G.P., and Popov A.N. A quantitative approach to data collection strategies. Acta Cryst D62 (2006) 58-64. Statistical modelling of all parameters in the diffraction experiment, including radiation damage, allowing rational optimization of data collection strategies.
    • (2006) Acta Cryst , vol.D62 , pp. 58-64
    • Bourenkov, G.P.1    Popov, A.N.2
  • 44
    • 0037317546 scopus 로고    scopus 로고
    • Specific radiation damage can be used to solve macromolecular crystal structures
    • Proof of principle of the viability of RIP for determining protein and DNA structures.
    • Ravelli R.B.G., Schrøder-Leiros H.K., Pan B., Caffrey M., and McSweeney S. Specific radiation damage can be used to solve macromolecular crystal structures. Structure Fold Des 11 (2003) 217-224. Proof of principle of the viability of RIP for determining protein and DNA structures.
    • (2003) Structure Fold Des , vol.11 , pp. 217-224
    • Ravelli, R.B.G.1    Schrøder-Leiros, H.K.2    Pan, B.3    Caffrey, M.4    McSweeney, S.5
  • 45
    • 16544391287 scopus 로고    scopus 로고
    • Determination of a novel structure by a combination of long-wavelength sulfur phasing and radiation-damage-induced phasing
    • Weiss M.S., Mander G., Hedderich R., Diederichs K., Ermler U., and Warkentin E. Determination of a novel structure by a combination of long-wavelength sulfur phasing and radiation-damage-induced phasing. Acta Cryst D60 (2004) 686-695
    • (2004) Acta Cryst , vol.D60 , pp. 686-695
    • Weiss, M.S.1    Mander, G.2    Hedderich, R.3    Diederichs, K.4    Ermler, U.5    Warkentin, E.6
  • 46
    • 33645963328 scopus 로고    scopus 로고
    • Phasing macromolecular structures with UV-induced structural changes
    • An elegant paper that describes how UV light can be used to inflict damage for RIP, therefore providing some advantages. These results pave the way for in-house UV-RIP structure determination.
    • Nanao M.H., and Ravelli R.B.G. Phasing macromolecular structures with UV-induced structural changes. Structure 14 (2006) 791-800. An elegant paper that describes how UV light can be used to inflict damage for RIP, therefore providing some advantages. These results pave the way for in-house UV-RIP structure determination.
    • (2006) Structure , vol.14 , pp. 791-800
    • Nanao, M.H.1    Ravelli, R.B.G.2
  • 47
    • 32944474426 scopus 로고    scopus 로고
    • Improving radiation-damage substructures for RIP
    • Nanao M.H., Sheldrick G.M., and Ravelli R.B.G. Improving radiation-damage substructures for RIP. Acta Cryst D61 (2005) 1227-1237
    • (2005) Acta Cryst , vol.D61 , pp. 1227-1237
    • Nanao, M.H.1    Sheldrick, G.M.2    Ravelli, R.B.G.3
  • 48
    • 16644361911 scopus 로고    scopus 로고
    • Expression, crystallization and crystallographic analysis of DegS, a stress sensor of the bacterial periplasm
    • Grininger M., Ravelli R.B.G., Heider U., and Zeth K. Expression, crystallization and crystallographic analysis of DegS, a stress sensor of the bacterial periplasm. Acta Cryst D60 (2004) 1429-1431
    • (2004) Acta Cryst , vol.D60 , pp. 1429-1431
    • Grininger, M.1    Ravelli, R.B.G.2    Heider, U.3    Zeth, K.4
  • 50
    • 27344443551 scopus 로고    scopus 로고
    • Biological imaging by soft X-ray diffraction microscopy
    • Landmark paper reporting the imaging of an intact and unstained yeast cell by soft X-ray diffraction microscopy.
    • Shapiro D., Thibault P., Beetz T., Elser V., Howells M., Jacobsen C., Kirz J., Lima E., Miao H., Neiman A.M., et al. Biological imaging by soft X-ray diffraction microscopy. Proc Natl Acad Sci USA 102 (2005) 15343-15346. Landmark paper reporting the imaging of an intact and unstained yeast cell by soft X-ray diffraction microscopy.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15343-15346
    • Shapiro, D.1    Thibault, P.2    Beetz, T.3    Elser, V.4    Howells, M.5    Jacobsen, C.6    Kirz, J.7    Lima, E.8    Miao, H.9    Neiman, A.M.10
  • 51
    • 33745822405 scopus 로고    scopus 로고
    • How to avoid premature decay of your macromolecular crystal: a quick soak for a long life
    • Kauffmann B., Weiss M.S., Lamzin V.S., and Schmidt A. How to avoid premature decay of your macromolecular crystal: a quick soak for a long life. Structure 14 (2006) 1099-1105
    • (2006) Structure , vol.14 , pp. 1099-1105
    • Kauffmann, B.1    Weiss, M.S.2    Lamzin, V.S.3    Schmidt, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.