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Instruments / Technical Area	Publication Details	Published
	Review of personnel safety systems at DLS M. C. Wilson 16th Int. Conf. on Accelerator and Large Experimental Control Systems ICALEPCS2017 DOI: 10.18429/JACoW-ICALEPCS2017-THPHA101 Open Access Show Abstract ▼ Abstract: Diamond Light Source is celebrating 10 years of "users" at its facility in Oxfordshire, England. Its safety systems have been designed to the standard EN61508, with the facility constructed in 3 phases, which are just concluding. The final "phase 3" beamline Personnel Safety System has been signed-off; hence it is timely to review our experience of the journey with these systems.	Jan 2018
Krios I-Titan Krios I at Diamond	Structural basis for the inhibition of RecBCD by Gam and its synergistic antibacterial effect with quinolones Martin Wilkinson , Lucy Troman , Wan Ak Wan Nur Ismah , Yuriy Chaban , Matthew B. Avison , Mark S. Dillingham , Dale B. Wigley Elife 5 DOI: 10.7554/eLife.22963 Open Access Show Abstract ▼ Abstract: Our previous paper (Wilkinson et al, 2016) used high-resolution cryo-electron microscopy to solve the structure of the Escherichia coli RecBCD complex, which acts in both the repair of double-stranded DNA breaks and the degradation of bacteriophage DNA. To counteract the latter activity, bacteriophage λ encodes a small protein inhibitor called Gam that binds to RecBCD and inactivates the complex. Here, we show that Gam inhibits RecBCD by competing at the DNA-binding site. The interaction surface is extensive and involves molecular mimicry of the DNA substrate. We also show that expression of Gam in E. coli or Klebsiella pneumoniae increases sensitivity to fluoroquinolones; antibacterials that kill cells by inhibiting topoisomerases and inducing double-stranded DNA breaks. Furthermore, fluoroquinolone-resistance in K. pneumoniae clinical isolates is reversed by expression of Gam. Together, our data explain the synthetic lethality observed between topoisomerase-induced DNA breaks and the RecBCD gene products, suggesting a new co-antibacterial strategy.	Dec 2016
Krios I-Titan Krios I at Diamond	Mechanism for nuclease regulation in RecBCD Martin Wilkinson , Yuriy Chaban , Dale B Wigley Elife 5 DOI: 10.7554/eLife.18227 Diamond Proposal Number(s): [13275] Open Access Show Abstract ▼ Abstract: In bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is catalysed by AddAB, AdnAB or RecBCD-type helicase-nucleases. These enzyme complexes are highly processive, duplex unwinding and degrading machines that require tight regulation. Here, we report the structure of E.coli RecBCD, determined by cryoEM at 3.8 Å resolution, with a DNA substrate that reveals how the nuclease activity of the complex is activated once unwinding progresses. Extension of the 5'-tail of the unwound duplex induces a large conformational change in the RecD subunit, that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit. The process involves a SH3 domain that binds to a region of the RecB subunit in a binding mode that is distinct from others observed previously in SH3 domains and, to our knowledge, this is the first example of peptide-binding of an SH3 domain in a bacterial system.	Sep 2016
I04-Macromolecular Crystallography	Structural basis for translocation by AddAB helicase-nuclease and its arrest at χ sites Wojciech Krajewski , Xin Fu , Martin Wilkinson , Nora Cronin , Mark S. Dillingham , Dale B. Wigley Nature DOI: 10.1038/nature13037 PMID: 24670664 Diamond Proposal Number(s): [8015] Show Abstract ▼ Abstract: In bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is dependent upon the recombination hotspot sequence χ (Chi)1, 2 and is catalysed by either an AddAB- or RecBCD-type helicase–nuclease (reviewed in refs 3, 4). These enzyme complexes unwind and digest the DNA duplex from the broken end until they encounter a χ sequence5, whereupon they produce a 3′ single-stranded DNA tail onto which they initiate loading of the RecA protein6. Consequently, regulation of the AddAB/RecBCD complex by χ is a key control point in DNA repair and other processes involving genetic recombination. Here we report crystal structures of Bacillus subtilis AddAB in complex with different χ-containing DNA substrates either with or without a non-hydrolysable ATP analogue. Comparison of these structures suggests a mechanism for DNA translocation and unwinding, suggests how the enzyme binds specifically to χ sequences, and explains how χ recognition leads to the arrest of AddAB (and RecBCD) translocation that is observed in single-molecule experiments	Mar 2014

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