Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography

A crystallogenesis study of human transthyretin using the counter-diffusion method is described as an alternative to conventional convective vapour diffusion and batch approaches for protein crystallization. The X-ray diffraction results show systematic trends that exhibit unique patterns of crystallization and high crystal quality as well as a remarkable degree of coherence within extended crystal rods that wholly fill the capillaries used. Preliminary neutron diffraction data have been recorded from a number of these samples, validating the feasibility of this methodology for neutron crystallography.

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Publication Details

Journal
Journal of Applied Crystallography
Published
2024-12-24
DOI
https://doi.org/10.1107/s1600576724011191
Primary Topic
Enzyme Structure and Function
Type
article
Field-Weighted Citation Impact
0.00

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article

Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography

Matthew P. Blakeley, Michael Haertlein, M.F. Oliva, Edward P. Mitchell et al.
Journal of Applied Crystallography
Enzyme Structure and Function
article

Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography

Matthew P. Blakeley, Michael Haertlein, M.F. Oliva, Edward P. Mitchell, Matthew W. Bowler, V. Trevor Forsyth, Martine Moulin, Clare De'Ath
article en

Abstract

A crystallogenesis study of human transthyretin using the counter-diffusion method is described as an alternative to conventional convective vapour diffusion and batch approaches for protein crystallization. The X-ray diffraction results show systematic trends that exhibit unique patterns of crystallization and high crystal quality as well as a remarkable degree of coherence within extended crystal rods that wholly fill the capillaries used. Preliminary neutron diffraction data have been recorded from a number of these samples, validating the feasibility of this methodology for neutron crystallography.

Journal of Applied CrystallographyVol. 58(1)
Consejo Superior de Investigaciones Científicas (ES), Lund University (SE), European Synchrotron Radiation Facility (FR), Xerox (France) (FR), Instituto Andaluz de Ciencias de la Tierra (ES), European Molecular Biology Laboratory (FR), Institut Laue-Langevin (FR), Institut de Biologie Structurale (FR)
Université Grenoble Alpes, Liam M. Kinne Foundation, Human Frontier Science Program, European Synchrotron Radiation Facility, Vetenskapsrådet, Ministerio de Ciencia e Innovación, French Infrastructure for Integrated Structural Biology, Erasmus+
Openalex Percentile: Top 84%
Enzyme Structure and Function
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Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography — Matthew P. Blakeley, Michael Haertlein, et al. · Journal of Applied Crystallography (2024) | TGRS Research Map | TGRS