Research Data Leeds Repository

Data Associated with 'Guanine Crystallization at Physiological pH'

Citation

Tah Roy, Bidisha and Hasselt, Lukas Jorin and Young, Ross and Yang, Zijiang and Williams, Jeanine and Galloway, Johanna M. and Heyam, Alex and Kim, Yi-Yeoun and Meldrum, Fiona C. (2025) Data Associated with 'Guanine Crystallization at Physiological pH'. University of Leeds. [Dataset] https://doi.org/10.5518/1552¹

Dataset description

Molecular organic crystals such as guanine are widely used by organisms for their remarkable optical properties. However, little is currently known about the mechanisms by which organisms control their formation, where efforts to elucidate these have been impeded by the very low solubility of these molecules in aqueous solutions at neutral pH. This creates significant challenges in crystallizing them under biologically-relevant conditions in the laboratory. Here, we introduce an enzymatic approach based on the purine metabolism process that yields significant quantities of guanine crystals in aqueous solution at neutral pH. The enzyme purine nucleoside phosphorylase (PNP) is used to continuously convert guanosine to guanine and generate supersaturation, and pure beta anhydrous guanine (β-AG) or alpha anhydrous guanine (α-AG) can be produced by changing the reagent concentrations or introducing stirring. Investigation of the reaction kinetics using high performance liquid chromatography (HPLC) and NMR reveals that the rate of change of supersaturation is crucial in determining the polymorph. This work bridges the gap between in vitro and biological crystallization and provides a facile means of studying the crystallization of biological molecules.

Keywords:

biomineralization, polymorph, molecular crystallization, bio-inspired, purines

Subjects:

F000 - Physical sciences > F100 - Chemistry²

Divisions:

Faculty of Engineering and Physical Sciences > School of Chemistry³

Related resources:

Location	Type
https://doi.org/10.1021/acs.cgd.5c00205⁴	Publication
https://eprints.whiterose.ac.uk/id/eprint/227661/⁵	Publication

License:

Creative Commons Attribution 4.0 International (CC BY 4.0)

Date deposited:

20 Jun 2025 14:51

URI:

https://archive.researchdata.leeds.ac.uk/id/eprint/1429⁶

Additional details

Creators or authors:

Creators	ORCID	Primary affiliation	Primary affiliation ID	Primary affiliation ID type
Tah Roy, Bidisha	https://orcid.org/0000-0003-0701-3050⁷	University of Leeds	https://ror.org/024mrxd33	ror
Hasselt, Lukas Jorin	https://orcid.org/0000-0002-8461-512X⁸	University of Leeds	https://ror.org/024mrxd33	ror
Young, Ross		University of Leeds	https://ror.org/024mrxd33	ror
Yang, Zijiang		University of Leeds	https://ror.org/024mrxd33	ror
Williams, Jeanine	https://orcid.org/0000-0003-2954-8339⁹	University of Leeds	https://ror.org/024mrxd33	ror
Galloway, Johanna M.	https://orcid.org/0000-0003-3998-0870¹⁰	University of Leeds	https://ror.org/024mrxd33	ror
Heyam, Alex	https://orcid.org/0000-0003-1569-5389¹¹	University of Leeds	https://ror.org/024mrxd33	ror
Kim, Yi-Yeoun	https://orcid.org/0000-0002-8503-4554¹²	University of Leeds	https://ror.org/024mrxd33	ror
Meldrum, Fiona C.	https://orcid.org/0000-0001-9243-8517¹³	University of Leeds	https://ror.org/024mrxd33	ror

Type of data:

Dataset

Research funders:

European Research Council, EPSRC, EPSRC

Grant numbers:

788968, EP/R018820/1, EP/T006331/1

Publication date:

2025

Resource language:

English

Metadata language:

English

Research project title:

DYNAMIN

Publisher:

University of Leeds

Contact email:

b.tah@leeds.ac.uk¹⁴

Last Modified:

20 Jun 2025 14:56

Files

Documentation

readme_TahRoy_DOI_1552.txt [4kB]

¹⁵

readme_TahRoy_DOI_1552.txt [4kB]

¹⁷

Data

STEM.zip [1MB]

¹⁹

STEM.zip [1MB]

²¹

HPLC.zip [5MB]

²³