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UV laser-excited fluorescence as a tool for the visualization of protein crystals mounted in loops.

Vernede X, Lavault B, Ohana J, Nurizzo D, Joly J, Jacquamet L, Felisaz F, Cipriani F, Bourgeois D
Acta Crystallogr D Biol Crystallogr 62 253-61 (2006)
Related entries: 2c8o, 2c8p, 2c8q

Cited: 15 times
EuropePMC logo PMID: 16510972

Abstract

Structural proteomics has promoted the rapid development of automated protein structure determination using X-ray crystallography. Robotics are now routinely used along the pipeline from genes to protein structures. However, a bottleneck still remains. At synchrotron beamlines, the success rate of automated sample alignment along the X-ray beam is limited by difficulties in visualization of protein crystals, especially when they are small and embedded in mother liquor. Despite considerable improvement in optical microscopes, the use of visible light transmitted or reflected by the sample may result in poor or misleading contrast. Here, the endogenous fluorescence from aromatic amino acids has been used to identify even tiny or weakly fluorescent crystals with a high success rate. The use of a compact laser at 266 nm in combination with non-fluorescent sample holders provides an efficient solution to collect high-contrast fluorescence images in a few milliseconds and using standard camera optics. The best image quality was obtained with direct illumination through a viewing system coaxial with the UV beam. Crystallographic data suggest that the employed UV exposures do not generate detectable structural damage.

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  1. Interaction between IGFBP7 and insulin: a theoretical and experimental study. Ruan W, Kang Z, Li Y, Sun T, Wang L, Liang L, Lai M, Wu T. Sci Rep 6 19586 (2016)


Reviews citing this publication (2)

  1. Automated technologies and novel techniques to accelerate protein crystallography for structural genomics. Manjasetty BA, Turnbull AP, Panjikar S, Büssow K, Chance MR. Proteomics 8 612-625 (2008)
  2. Synergy within structural biology of single crystal optical spectroscopy and X-ray crystallography. De la Mora-Rey T, Wilmot CM. Curr Opin Struct Biol 17 580-586 (2007)

Articles citing this publication (12)

  1. The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin. Schönfeld DL, Ravelli RB, Mueller U, Skerra A. J Mol Biol 384 393-405 (2008)
  2. Crystallophore: a versatile lanthanide complex for protein crystallography combining nucleating effects, phasing properties, and luminescence. Engilberge S, Riobé F, Di Pietro S, Lassalle L, Coquelle N, Arnaud CA, Pitrat D, Mulatier JC, Madern D, Breyton C, Maury O, Girard E. Chem Sci 8 5909-5917 (2017)
  3. The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist. Rudiño-Piñera E, Ravelli RB, Sheldrick GM, Nanao MH, Korostelev VV, Werner JM, Schwarz-Linek U, Potts JR, Garman EF. J Mol Biol 368 833-844 (2007)
  4. To automate or not to automate: this is the question. Cymborowski M, Klimecka M, Chruszcz M, Zimmerman MD, Shumilin IA, Borek D, Lazarski K, Joachimiak A, Otwinowski Z, Anderson W, Minor W. J Struct Funct Genomics 11 211-221 (2010)
  5. Dynamic X-ray diffraction sampling for protein crystal positioning. Scarborough NM, Godaliyadda GM, Ye DH, Kissick DJ, Zhang S, Newman JA, Sheedlo MJ, Chowdhury AU, Fischetti RF, Das C, Buzzard GT, Bouman CA, Simpson GJ. J Synchrotron Radiat 24 188-195 (2017)
  6. DeepCentering: fully automated crystal centering using deep learning for macromolecular crystallography. Ito S, Ueno G, Yamamoto M. J Synchrotron Radiat 26 1361-1366 (2019)
  7. A visible-light-excited fluorescence method for imaging protein crystals without added dyes. Lukk T, Gillilan RE, Szebenyi DM, Zipfel WR. J Appl Crystallogr 49 234-240 (2016)
  8. Crystallization of Enantiomerically Pure Proteins from Quasi-Racemic Mixtures: Structure Determination by X-Ray Diffraction of Isotope-Labeled Ester Insulin and Human Insulin. Mandal K, Dhayalan B, Avital-Shmilovici M, Tokmakoff A, Kent SB. Chembiochem 17 421-425 (2016)
  9. Quantitive evaluation of macromolecular crystallization experiments using 1,8-ANS fluorescence. Watts D, Müller-Dieckmann J, Tsakanova G, Lamzin VS, Groves MR. Acta Crystallogr D Biol Crystallogr 66 901-908 (2010)
  10. Spectroscopic studies of model photo-receptors: validation of a nanosecond time-resolved micro-spectrophotometer design using photoactive yellow protein and α-phycoerythrocyanin. Purwar N, Tenboer J, Tripathi S, Schmidt M. Int J Mol Sci 14 18881-18898 (2013)
  11. Exploiting Microbeams for Membrane Protein Structure Determination. Warren AJ, Axford D, Paterson NG, Owen RL. Adv Exp Med Biol 922 105-117 (2016)
  12. Depth-of-field extension in optical imaging for rapid crystal screening. Li C, Ding C, Li M, Rong J, Florian H, Simpson G. Acta Crystallogr D Struct Biol 77 463-470 (2021)


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