RAS PhysicsКристаллография Crystallography Reports

  • ISSN (Print) 0023-4761
  • ISSN (Online) 3034-5510

EFFECT OF SOLVENT ISOTOPE COMPOSITION (HO AND DO) ON LYSOZYME OLIGOMER FORMATION UNDER CRYSTALLIZATION CONDITIONS

PII
S3034551025060044-1
DOI
10.7868/S3034551025060044
Publication type
Article
Status
Published
Authors
Volume/ Edition
Volume 70 / Issue number 6
Pages
917-924
Abstract
Using the method of small-angle X-ray scattering (SAXS), the temperature dependencies (in the range of 4 to 30°C with a 1°C step) of the structure of a lysozyme solution during the growth of tetragonal crystals were obtained for HO and DO solvents. It was found that, regardless of the solvent type, dimers and octamers form in the lysozyme crystallization solution. The volume fractions of the oligomers (dimers and octamers) are inversely proportional to the temperature change, both in the case of the HO solvent and the DO solvent. Under identical temperature conditions, the volume fraction of oligomers in the lysozyme crystallization solution in DO is approximately 8% higher than in HO. However, the same oligomer content in the lysozyme crystallization solutions in HO and DO is achieved when the temperature of the HO solution is approximately 10°C lower than that of the DO solution. This may be explained by the distinct influence of the solvent on protein hydration.
Keywords
Date of publication
15.09.2025
Year of publication
2025
Number of purchasers
0
Views
5

References

  1. 1. McPherson A., Cudney B. // Acta Cryst. F. 2014. V. 70. № 11. P. 1445. https://doi.org/10.1107/S2053230X14019670
  2. 2. Luft J.R., Newman J., Snell E.H. // Acta Cryst. F. 2014. V. 70. № 7. P. 835. https://doi.org/10.1107/S2053230X1401262X
  3. 3. Zhang C.Y., Wu Z.Q., Yin et al. // Acta Cryst. F. 2013. V. 9. № 7. P. 821. https://doi.org/10.1107/S1744309113013651
  4. 4. Astier J.P., Veesler S. // Cryst. Growth Des. 2008. V. 8. № 12. P. 4215. https://doi.org/10.1021/cg800665b
  5. 5. Бойкова А.С., Дьякова Ю.А., Ильина К.Б. и др. // Кристаллография. 2017. Т. 62. № 6. С. 876. https://doi.org/10.7868/S0023476117060078
  6. 6. Марченкова М.А., Конарев П.В., Бойкова А.С. и др. // Кристаллография. 2021. Т. 66. № 5. С. 723. https://doi.org/10.31857/S0023476121050131
  7. 7. Marchenkova M.A., Konarev P.V., Kordonskaya Yu.V. et al. // Crystals. 2022. V. 12. P. 751. https://doi.org/10.3390/cryst12060751
  8. 8. Марченкова М.А., Бойкова А.С., Ильина К.Б. и др. // Acta Naturae. 2023. Т. 15. № 1. С. 58. https://doi.org/10.7868/S0023476117060078
  9. 9. De Yoreo J.J., Gilbert P.U., Sommerdijk N.A. et al. // Science. 2015. V. 349. P. aaa6760. https://doi.org/10.1126/science.aaa6760
  10. 10. Sukhanov A.E., Konarev P.V., Timofeev V.I. et al. // Crystals. 2023. V. 13. P. 1577. https://doi.org/10.3390/cryst13111577
  11. 11. Tanaka S., Ito K., Hayakawa R. et al. // J. Chem. Phys. 1999. V. 111. № 22. P. 10330. https://doi.org/10.1063/1.480381
  12. 12. Niimura N., Minezaki Y., Ataka M. et al. // J. Cryst. Growth. 1995. V. 154. P. 136. https://doi.org/10.1016/0022-0248 (95)00164-6
  13. 13. Ducruix A., Guilloteau J.-P., Riès-Kautt M. et al. // J. Cryst. Growth. 1996. V. 168. № 1–4. P. 28. https://doi.org/10.1016/0022-0248 (96)00359-4
  14. 14. Giubertoni G., Bakker H.J., Russo D. // J. Phys. Chem. B. 2023. V. 127. P. 5678. https://doi.org/10.1021/acs.jpcb.3c04385
  15. 15. Stefaniuk A. // Sci. Rep. 2022. V. 12. P. 23551. https://doi.org/10.1038/s41598-022-23551-9
  16. 16. Bielskutė S. // Protein Sci. 2021. V. 30. P. 2181. https://doi.org/10.1002/pro.4110
  17. 17. Tempra C., Sibani L., Hansen F.Y. et al. // J. Phys. Chem. B. 2023. V. 127. P. 5678. https://doi.org/10.1021/acs.jpcb.2c08270
  18. 18. Banks H., Beck C., Buchholz C. et al. // Cryst. Growth Des. 2025. V. 25. P. 5174. https://doi.org/10.1021/acs.cgd.5c00116
  19. 19. Pernot P., Round A., Barrett R. et al. // J. Synchrotron Radiat. 2013. V. 20. P. 660. https://doi.org/10.1107/S0909049513010431
  20. 20. Round A., Felisaz F., Fodinger L. et al. // Acta Cryst. D. 2015. V. 71. P. 67. https://doi.org/10.1107/S1399004714026959
  21. 21. Brennich M.E., Kieffer J., Bonamis G. et al. // J. Appl. Cryst. 2016. V. 49. P. 203. https://doi.org/10.1107/S1600576715024462
  22. 22. Konarev P.V., Volkov V.V., Sokolova A.V. et al. // J. Appl. Cryst. 2003. V. 36. P. 1277. https://doi.org/10.1107/S0021889803012779
  23. 23. Franke D., Petoukhov M.V., Konarev P.V. et al. // J. Appl. Cryst. 2017. V. 50. P. 1212. https://doi.org/10.1107/S1600576717007786
  24. 24. Svergun D.I., Barberato C., Koch M.H.J. //J. Appl. Cryst. 1995. V. 28. P. 768. https://doi.org/10.1107/S0021889895007047
  25. 25. Goryunov A.S. // Gen. Physiol. Biophys. 2006. V. 25. P. 303.
  26. 26. Kresheck G.C., Schneider H., Scheraga H.A. // J. Phys. Chem. 1965. V. 69. P. 3132. https://doi.org/10.1021/j100893a054
  27. 27. Gripon C., Legrand L., Rosenman I. et al. // J. Cryst. Growth. 1997. V. 177. P. 238. https://doi.org/10.1016/S0022-0248 (96)01077-9
QR
Translate

Indexing

Scopus

Scopus

Scopus

Crossref

Scopus

Higher Attestation Commission

At the Ministry of Education and Science of the Russian Federation

Scopus

Scientific Electronic Library