Crossref journal-article
Royal Society of Chemistry (RSC)
Faraday Discussions (292)
Abstract

We report a real-time study on protein crystallization in the presence of multivalent salts using small angle X-ray scattering (SAXS) and optical microscopy, focusing particularly on the nucleation mechanism as well as on the role of the metastable intermediate phase (MIP). Using bovine beta-lactoglobulin as a model system in the presence of the divalent salt CdCl2, we have monitored the early stage of crystallization kinetics which demonstrates a two-step nucleation mechanism: protein aggregates form a MIP, which is followed by the nucleation of crystals within the MIP. Here we focus on characterizing and tuning the structure of the MIP using salt and the related effects on the two-step nucleation kinetics. The results suggest that increasing the salt concentration near the transition zonepseudo-c** enhances the energy barrier for both MIPs and crystal nucleation, leading to slow growth. The structural evolution of the MIP and its effect on subsequent nucleation is discussed based on the growth kinetics. The observed kinetics can be well described, using a rate-equation model based on a clear physical two-step picture. This real-time study not only provides evidence for a two-step nucleation process for protein crystallization, but also elucidates the role and the structural signature of the MIPs in the nonclassical process of protein crystallization.

Bibliography

Sauter, A., Roosen-Runge, F., Zhang, F., Lotze, G., Feoktystov, A., Jacobs, R. M. J., & Schreiber, F. (2015). On the question of two-step nucleation in protein crystallization. Faraday Discussions, 179, 41–58.

Authors 7
  1. Andrea Sauter (first)
  2. Felix Roosen-Runge (additional)
  3. Fajun Zhang (additional)
  4. Gudrun Lotze (additional)
  5. Artem Feoktystov (additional)
  6. Robert M. J. Jacobs (additional)
  7. Frank Schreiber (additional)
References 53 Referenced 61
  1. 10.1021/ja1051445 / J. Am. Chem. Soc. by Jacobson (2010)
  2. H. Cölfen and M.Antonietti, Mesocrystals and nonclassical crystallization, John Wiley & Sons, West Sussex, 2008 (10.1002/9780470994603) / Mesocrystals and nonclassical crystallization by Cölfen (2008)
  3. 10.1126/science.1164271 / Science by Gebauer (2008)
  4. 10.1039/C3CS60451A / Chem. Soc. Rev. by Gebauer (2014)
  5. 10.1126/science.1230915 / Science by Wallace (2013)
  6. 10.1179/1743280411Y.0000000015 / Int. Mater. Rev. by Sear (2012)
  7. 10.1021/ja043218k / J. Am. Chem. Soc. by Gliko (2005)
  8. 10.1021/jp068827o / J. Phys. Chem. B by Gliko (2007)
  9. 10.1529/biophysj.106.094854 / Biophys. J. by Pan (2007)
  10. 10.1021/jp100617w / J. Phys. Chem. B by Pan (2010)
  11. 10.1016/S0006-3495(04)74239-3 / Biophys. J. by Chen (2004)
  12. 10.1021/cg900919w / Cryst. Growth Des. by Liu (2010)
  13. 10.1103/PhysRevLett.105.025701 / Phys. Rev. Lett. by Schilling (2010)
  14. 10.1126/science.277.5334.1975 / Science by Wolde (1997)
  15. 10.1063/1.2761891 / J. Chem. Phys. by Hutchens (2007)
  16. 10.1103/PhysRevLett.107.175702 / Phys. Rev. Lett. by Tóth (2011)
  17. 10.1103/PhysRevLett.96.175701 / Phys. Rev. Lett. by Schöpe (2006)
  18. 10.1021/ja073598k / J. Am. Chem. Soc. by Zhang (2007)
  19. 10.1103/PhysRevLett.102.198302 / Phys. Rev. Lett. by Savage (2009)
  20. 10.1073/pnas.1309320111 / Proc. Natl. Acad. Sci. U. S. A. by Sleutel (2014)
  21. 10.1002/cbic.201402597 / ChemBioChem by Bijelic (2015)
  22. 10.1039/a809346f / Phys. Chem. Chem. Phys. by Rein ten Wolde (1999)
  23. 10.1021/cg049977w / Cryst. Growth Des. by Vekilov (2004)
  24. 10.1038/nphys2817 / Nat. Phys. by Tan (2014)
  25. 10.1038/nmat4083 / Nat. Mater. by Peng (2015)
  26. 10.1073/pnas.1001040107 / Proc. Natl. Acad. Sci. U. S. A. by Kawasaki (2010)
  27. 10.1103/PhysRevLett.96.046102 / Phys. Rev. Lett. by Lutsko (2006)
  28. 10.1016/j.cocis.2004.01.008 / Curr. Opin. Colloid Interface Sci. by Piazza (2004)
  29. 10.1016/j.cocis.2005.09.003 / Curr. Opin. Colloid Interface Sci. by Sear (2006)
  30. 10.1021/jp0649955 / J. Phys. Chem. B by Zhang (2007)
  31. 10.1021/ja510533x / J. Am. Chem. Soc. by Sauter (2015)
  32. H. A. Sober , CRC Handbook of Biochemistry: Selected data for molecular biology, CRC, 1970 / CRC Handbook of Biochemistry: Selected data for molecular biology by Sober (1970)
  33. 10.1021/la9601061 / Langmuir by Elofsson (1997)
  34. 10.1002/prot.22852 / Proteins: Struct., Funct., Bioinf. by Zhang (2010)
  35. T. Narayanan , Synchrotron small-angle X-ray scattering, in Soft Matter Characterization, ed. R. Borsali and R. Pecora, Springer, 2008, p. 899ff / Soft Matter Characterization by Narayanan (2008)
  36. V. Pipich, QtiKWS: user-friendly program for reduction, visualization, analysis and fit of SA(N)S data, http://www.qtikws.de, 2012
  37. 10.1103/PhysRevLett.101.148101 / Phys. Rev. Lett. by Zhang (2008)
  38. 10.1107/S0021889811017997 / J. Appl. Crystallogr. by Zhang (2011)
  39. 10.1039/C2SM07008A / Soft Matter by Zhang (2012)
  40. 10.1515/pac-2014-5002 / Pure Appl. Chem. by Zhang (2014)
  41. 10.1021/jp401874t / J. Phys. Chem. B by Roosen-Runge (2013)
  42. 10.1021/jp5058622 / J. Phys. Chem. B by Jordan (2014)
  43. 10.1039/C3SM52447G / Soft Matter by Soraruf (2014)
  44. 10.1038/srep07016 / Sci. Rep. by Roosen-Runge (2014)
  45. 10.1103/PhysRevLett.108.186101 / Phys. Rev. Lett. by Kubíčková (2012)
  46. 10.1143/JPSJ.80.123602 / J. Phys. Soc. Jpn. by Akiyama (2011)
  47. 10.1021/cg501099d / Cryst. Growth Des. by Sauter (2014)
  48. 10.1021/jp9112156 / J. Phys. Chem. B by Ianeselli (2010)
  49. 10.1002/(SICI)1097-0282(199901)49:1<11::AID-BIP2>3.0.CO;2-1 / Biopolymers by Verheul (1999)
  50. 10.1039/c2fd20021j / Faraday Discuss. by Zhang (2012)
  51. 10.2142/biophysics.6.1 / Biophysics by Sato (2010)
  52. 10.1039/c2cp23460b / Phys. Chem. Chem. Phys. by Zhang (2012)
  53. G. Strobl , in The physics of polymers, Springer, Berlin, Heidelberg, New York, 3rd edn, 2007, ch. 5 / The physics of polymers by Strobl (2007)
Dates
Type When
Created 10 years, 7 months ago (Jan. 12, 2015, 6:03 a.m.)
Deposited 1 year, 4 months ago (April 17, 2024, 1:22 p.m.)
Indexed 19 hours, 13 minutes ago (Aug. 21, 2025, 1:24 p.m.)
Issued 10 years, 7 months ago (Jan. 1, 2015)
Published 10 years, 7 months ago (Jan. 1, 2015)
Published Online 10 years, 7 months ago (Jan. 1, 2015)
Funders 1
  1. Deutsche Forschungsgemeinschaft 10.13039/501100001659

    Region: Europe

    gov (National government)

    Labels3
    1. German Research Association
    2. German Research Foundation
    3. DFG
    Awards1
    1. ZH226/3-1

@article{Sauter_2015, title={On the question of two-step nucleation in protein crystallization}, volume={179}, ISSN={1364-5498}, url={http://dx.doi.org/10.1039/c4fd00225c}, DOI={10.1039/c4fd00225c}, journal={Faraday Discussions}, publisher={Royal Society of Chemistry (RSC)}, author={Sauter, Andrea and Roosen-Runge, Felix and Zhang, Fajun and Lotze, Gudrun and Feoktystov, Artem and Jacobs, Robert M. J. and Schreiber, Frank}, year={2015}, pages={41–58} }