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Instruments / Technical Area	Publication Details	Published
	Advances in cryo-electron tomography and subtomogram averaging and classification Peijun Zhang Current Opinion In Structural Biology DOI: 10.1016/j.sbi.2019.05.021 Open Access Show Abstract ▼ Abstract: Cryo-electron tomography (cryoET) can provide 3D reconstructions, or tomograms, of pleomorphic objects such as organelles or cells in their close-to-native states. Subtomograms that contain repetitive structures can be further extracted and subjected to averaging and classification to improve resolution, and this process has become an emerging structural biology method referred to as cryoET subtomogram averaging and classification (cryoSTAC). Recent technical advances in cryoSTAC have had a profound impact on many fields in biology. Here, I review recent exciting work on several macromolecular assemblies demonstrating the power of cryoSTAC for in situ structure analysis and discuss challenges and future directions.	Jul 2019
I03-Macromolecular Crystallography	Metallocofactor assembly for [FeFe]-hydrogenases Pedro Dinis , Beata M. Wieckowski , Peter L. Roach Current Opinion In Structural Biology 41, 90 - 97 DOI: 10.1016/j.sbi.2016.06.004 Diamond Proposal Number(s): [8889] Show Abstract ▼ Abstract: Hydrogenases are a potential source of environmentally benign bioenergy, using complex cofactors to catalyze the reversible reduction of protons to form hydrogen. The most active subclass, the [FeFe]-hydrogenases, is dependent on a metallocofactor, the H cluster, that consists of a two iron subcluster ([2Fe]H) bridging to a classical cubane cluster ([4Fe–4S]H). The ligands coordinating to the diiron subcluster include an azadithiolate, three carbon monoxides, and two cyanides. To assemble this complex cofactor, three maturase enzymes, HydG, HydE and HydF are required. The biosynthesis of the diatomic ligands proceeds by an unusual fragmentation mechanism, and structural studies in combination with spectroscopic analysis have started to provide insights into the HydG mediated assembly of a [2Fe]H subcluster precursor.	Dec 2016
I02-Macromolecular Crystallography I03-Macromolecular Crystallography I04-Macromolecular Crystallography	The structural biology of patellamide biosynthesis Jesko Koehnke , Andrew Bent , Wael E Houssen , Greg Mann , Marcel Jaspars , James Naismith Current Opinion In Structural Biology 29, 112 - 121 DOI: 10.1016/j.sbi.2014.10.006 Diamond Proposal Number(s): [8268] Open Access Show Abstract ▼ Abstract: The biosynthetic pathways for patellamide and related natural products have recently been studied by structural biology. These pathways produce molecules that have a complex framework and exhibit a diverse array of activity due to the variability of the amino acids that are found in them. As these molecules are difficult to synthesize chemically, exploitation of their properties has been modest. The patellamide pathway involves amino acid heterocyclization, peptide cleavage, peptide macrocyclization, heterocycle oxidation and epimerization; closely related products are also prenylated. Enzyme activities have been identified for all these transformations except epimerization, which may be spontaneous. This review highlights the recent structural and mechanistic work on amino acid heterocyclization, peptide cleavage and peptide macrocyclization. This work should help in using the enzymes to produce novel analogs of the natural products enabling an exploitation of their properties.	Dec 2014
	Micro-crystallography comes of age Janet L. Smith , Robert F. Fischetti , Masaki Yamamoto Current Opinion In Structural Biology 22 (5), 602 - 612 DOI: 10.1016/j.sbi.2012.09.001 Show Abstract ▼ Abstract: X-ray micro-beams permit structure determination from small or imperfect crystals; Robust micro-beams require source; optics and sample support to be extremely stable; Four different approaches to making a 1-20 um beam have been implemented; A growing demand has led to about 20 beamlines for micro-crystallography worldwide; Micro-beams enable data collection from LCP-grown crystals and crystals in situ.	Oct 2012
I02-Macromolecular Crystallography I04-Macromolecular Crystallography	Structural insights into the retroviral DNA integration apparatus Peter Cherepanov , Goedele Maertens , Stephen Hare Current Opinion In Structural Biology 21 (2), 249 - 256 DOI: 10.1016/j.sbi.2010.12.005 PMID: 21277766 Diamond Proposal Number(s): [317] Show Abstract ▼ Abstract: Retroviral replication depends on successful integration of the viral genetic material into a host cell chromosome. Virally encoded integrase, an enzyme from the DDE(D) nucleotidyltransferase superfamily, is responsible for the key DNA cutting and joining steps associated with this process. Insights into the structural and mechanistic aspects of integration are directly relevant for the development of antiretroviral drugs. Recent breakthroughs have led to biochemical and structural characterization of the principal integration intermediates revealing the tetramer of integrase that catalyzes insertion of both 3' viral DNA ends into a sharply bent target DNA. This review discusses the mechanism of retroviral DNA integration and the mode of action of HIV-1 integrase strand transfer inhibitors in light of the recent visualization of the prototype foamy virus intasome, target DNA capture and strand transfer complexes.	Apr 2011
B23-Circular Dichroism	The conformation and structure of GAGs: recent progress and perspectives T. R. Rudd , M. A. Skidmore , M. Guerrini , M. Hricovini , A. K. Powell , G. Siligardi , E. A. Yates Current Opinion In Structural Biology DOI: 10.1016/j.sbi.2010.08.004 Show Abstract ▼ Abstract: The glycosaminoglycan (GAG) family of linear sulphated polysaccharides are involved in most regulatory processes in the extracellular matrix of higher organisms. The relationship between GAG substitution pattern and activity, however, remains unclear and experimental evidence suggests that subtle conformational factors play an important role. The difficulty of modelling these complex charged molecules shifts the burden of investigation towards experimental techniques. Recent advances in complementary physical-chemical, particularly spectroscopy-based approaches are reviewed, together with methods for analysing the resulting complex data. The prospects for combining some of these approaches and fitting them into the wider context of interactions, are also discussed.	Sep 2010
NONE-No attached Diamond beamline	Overcoming the challenges of membrane protein crystallography. Liz Carpenter , Konstantinos Beis , So Iwata , Alex Cameron Current Opinion In Structural Biology 18(5), 581-6 DOI: 10.1016/j.sbi.2008.07.001 PMID: 18674618 Open Access Show Abstract ▼ Abstract: Membrane protein structural biology is still a largely unconquered area, given that approximately 25% of all proteins are membrane proteins and yet less than 150 unique structures are available. Membrane proteins have proven to be difficult to study owing to their partially hydrophobic surfaces, flexibility and lack of stability. The field is now taking advantage of the high-throughput revolution in structural biology and methods are emerging for effective expression, solubilisation, purification and crystallisation of membrane proteins. These technical advances will lead to a rapid increase in the rate at which membrane protein structures are solved in the near future.	Oct 2008
	Transport mechanism of the sarcoplasmic reticulum Ca2+-ATPase pump Jesper Moller , Poul Nissen , Thomas Sorensen , Marc Le Maire Current Opinion In Structural Biology 15 (4), 387-393 DOI: 10.1016/j.sbi.2005.06.005 Show Abstract ▼ Abstract: The sarcoplasmic reticulum Ca2+-ATPase (SERCA1a) belongs to the group of P-type ATPases, which actively transport inorganic cations across membranes at the expense of ATP hydrolysis. Three-dimensional structures of several transport intermediates of SERCA1a, stabilized by structural analogues of ATP and phosphoryl groups, are now available at atomic resolution. This has enabled the transport cycle of the protein to be described, including the coupling of Ca2+ occlusion and phosphorylation by ATP, and of proton counter-transport and dephosphorylation. From these structures, Ca2+-ATPase gradually emerges as a molecular mechanical device in which some of the transmembrane segments perform Ca2+ transport by piston-like movements and by the transmission of reciprocating movements that affect the chemical reactivity of the cytosolic globular domains.	Jul 2005

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