Neutron diffraction techniques permit direct determination of the hydrogen (H) and deuterium (D) positions in crystal structures of biological macromolecules at resolutions of ∼1.5 and 2.5 Å, respectively. In addition, neutron diffraction data can be collected from a single crystal at room temperature without radiation damage issues. By locating the positions of H/D-atoms, protonation states and water molecule orientations can be determined, leading to a more complete understanding of many biological processes and drug-binding. In the last ca. 5 years, new beamlines have come online at reactor neutron sources, such as BIODIFF at Heinz Maier-Leibnitz Zentrum and IMAGINE at Oak Ridge National Laboratory (ORNL), and at spallation neutron sources, such as MaNDi at ORNL and iBIX at the Japan Proton Accelerator Research Complex. In addition, significant improvements have been made to existing beamlines, such as LADI-III at the Institut Laue-Langevin. The new and improved instrumentations are allowing sub-mm3 crystals to be regularly used for data collection and permitting the study of larger systems (unit-cell edges >100 Å). Owing to this increase in capacity and capability, many more studies have been performed and for a wider range of macromolecules, including enzymes, signalling proteins, transport proteins, sugar-binding proteins, fluorescent proteins, hormones and oligonucleotides; of the 126 structures deposited in the Protein Data Bank, more than half have been released since 2013 (65/126, 52%). Although the overall number is still relatively small, there are a growing number of examples for which neutron macromolecular crystallography has provided the answers to questions that otherwise remained elusive.
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April 2018
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Cryo-STX projection image showing a parasitophorous vacuole (yellow) within a human fibroblast cell, containing four Toxoplasma gondii parasites (membranes in cyan, nuclei in red and rhoptries in green). In this issue of Emerging Topics in Life Sciences, Harkiolaki et al. describe the use of Cryo-soft X-ray tomography to explore the ultrastructure of whole cells. Image kindly provided by Professor Helen Saibil (Birkbeck College, London, U.K.). For further details, see pages 81–92.
Review Article|
February 16 2018
Neutron macromolecular crystallography
Matthew P. Blakeley
;
Matthew P. Blakeley
1Large-Scale Structures Group, Institut Laue-Langevin, 71 Avenue des Martyrs, Grenoble 38000, France
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Alberto D. Podjarny
2Department of Integrative Biology, IGBMC, CNRS, INSERM, Université de Strasbourg, Illkirch, France
Correspondence: Alberto D. Podjarny (apodjarny@gmail.com)
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Emerg Top Life Sci (2018) 2 (1): 39–55.
Article history
Received:
October 27 2017
Revision Received:
December 12 2017
Accepted:
December 19 2017
Citation
Marcellus Ubbink, Anastassis Perrakis, Matthew P. Blakeley, Alberto D. Podjarny; Neutron macromolecular crystallography. Emerg Top Life Sci 20 April 2018; 2 (1): 39–55. doi: https://doi.org/10.1042/ETLS20170083
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