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Instruments / Technical Area	Publication Details	Published
B21-High Throughput SAXS	Structural analysis of the partially disordered protein EspK from Mycobacterium tuberculosis Abril Gijsbers , Nuria Sánchez-Puig , Ye Gao , Peter J. Peters , Raimond B. G. Ravelli , Dritan Siliqi Crystals 11 DOI: 10.3390/cryst11010018 Diamond Proposal Number(s): [21741, 21035] Open Access Show Abstract ▼ Abstract: For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker.	Dec 2020
I22-Small angle scattering & Diffraction	Large multimeric assemblies of nucleosome assembly protein and histones revealed by small-angle X-ray scattering and electron microscopy E. R. Newman , G. G. Kneale , R. B. G. Ravelli , M. Karuppasamy , F. K. Nejadasl , I. A. Taylor , J. E. Mcgeehan Journal Of Biological Chemistry DOI: 10.1074/jbc.M112.340422 Show Abstract ▼ Abstract: The nucleosome assembly protein (NAP) family represents a key group of histone chaperones that are essential for cell viability. Several x-ray structures of NAP1 dimers are available; however, there are currently no structures of this ubiquitous chaperone in complex with histones. We have characterized NAP1 from Xenopus laevis and reveal that it forms discrete multimers with histones H2A/H2B and H3/H4 at a stoichiometry of one NAP dimer to one histone fold dimer. These complexes have been characterized by size exclusion chromatography, analytical ultracentrifugation, multiangle laser light scattering, and small-angle x-ray scattering to reveal their oligomeric assembly states in solution. By employing single-particle cryo-electron microscopy, we visualized these complexes for the first time and show that they form heterogeneous ring-like structures, potentially acting as large scaffolds for histone assembly and exchange.	Jun 2012
	Improving diffraction by humidity control: a novel device compatible with X-ray beamlines Matthew W. Bowler , Julien Huet , Alexandre Gobbo , Franck Felisaz , Bernard Lavault , Raphael Moya , Jan Kadlec , Raimond Ravelli , Florent Cipriani , Juan Sanchez-Weatherby Acta Crystallographica Section D Biological Crystallography 65 (12), 1237-1246 DOI: 10.1107/S0907444909037822 PMID: 19966409 Show Abstract ▼ Abstract: Dehydration of protein crystals is rarely used, despite being a post-crystallization method that is useful for the improvement of crystal diffraction properties, as it is difficult to reproduce and monitor. A novel device for hydration control of macromolecular crystals in a standard data-collection environment has been developed. The device delivers an air stream of precise relative humidity that can be used to alter the amount of water in macromolecular crystals. The device can be rapidly installed and is fully compatible with most standard synchrotron X-ray beamlines. Samples are mounted in cryoloops and the progress of dehydration can be monitored both optically and by the acquisition of diffraction images. Once the optimal hydration level has been obtained, cryocooling is easy to achieve by hand or by using a sample changer. The device has been thoroughly tested on several ESRF beamlines and is available to users.	Dec 2009

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