Imperial College London

DrJamesMurray

Faculty of Natural SciencesDepartment of Life Sciences

Senior Lecturer
 
 
 
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Contact

 

+44 (0)20 7594 8895j.w.murray Website

 
 
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Location

 

724Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Publication Type
Year
to

56 results found

McFarlane C, Shah N, Kabasakal B, Echeverria B, Cotton C, Bubeck D, Murray Jet al., 2019, Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria, Proceedings of the National Academy of Sciences of USA, Vol: 116, Pages: 20984-20990, ISSN: 0027-8424

Plants, algae, and cyanobacteria fix carbon dioxide to organic carbon with the Calvin-Benson (CB) cycle. Phosphoribulokinase (PRK) and glyceraldehyde 3 phosphate dehydrogenase (GAPDH) are essential Calvin-Benson cycle enzymes that control substrate availability for the carboxylation enzyme Rubisco. PRK consumes ATP to produce the Rubisco substrate ribulose bisphosphate (RuBP). GAPDH catalyses the reduction step of the CB cycle with NADPH to produce the sugar, glyceraldehyde 3-phosphate (GAP), which is used for regeneration of RuBP and is the main exit point of the cycle. GAPDH and PRK are co-regulated by the redox state of a conditionally disordered protein CP12, which forms a ternary complex with both enzymes. However, the structural basis of Calvin-Benson cycle regulation by CP12 is unknown. Here we show how CP12 modulates the activity of both GAPDH and PRK. Using thermophilic cyanobacterial homologues, we solve crystal structures of GAPDH with different cofactors and CP12 bound, and the ternary GAPDH-CP12-PRK complex by electron cryo-microscopy, we reveal that formation of the N-terminal disulfide pre-orders CP12 prior to binding the PRK active site, which is resolved in complex with CP12. We find that CP12 binding to GAPDH influences substrate accessibility of all GAPDH active sites in the binary and ternary inhibited complexes. Our structural and biochemical data explain how CP12 integrates responses from both redox state and nicotinamide dinucleotide availability to regulate carbon fixation.

Journal article

Varghese F, Kabasakal BV, Cotton CA, Schumacher J, Rutherford AW, Fantuzzi A, Murray JWet al., 2019, A low-potential terminal oxidase associated with the iron-only nitrogenase from the nitrogen-fixing bacterium Azotobacter vinelandii, Journal of Biological Chemistry, ISSN: 0021-9258

The biological route for nitrogen gas entering the biosphere is reduction to ammonia by the nitrogenase enzyme, which is inactivated by oxygen. Three types of nitrogenase exist, the least studied of which is the iron-only nitrogenase. The Anf3 protein in the bacterium Rhodobacter capsulatus is essential for diazotrophic (i.e. nitrogen-fixing) growth with the iron-only nitrogenase, but its enzymatic activity and function are unknown. Here, we biochemically and structurally characterize Anf3 from the model diazotrophic bacterium Azotobacter vinelandii. Determining the Anf3 crystal structure to atomic resolution, we observed that it is a dimeric flavocytochrome with an unusually close interaction between the heme and the flavin adenine dinucleotide cofactors. Measuring the reduction potentials by spectroelectrochemical redox titration, we observed values of -420 ± 10 mV and -330 ± 10 mV for the two FAD potentials and -340 ± 1 mV for the heme. We further show that Anf3 accepts electrons from spinach ferredoxin and that Anf3 consumes oxygen without generating superoxide or hydrogen peroxide. We predict that Anf3 protects the iron-only nitrogenase from oxygen inactivation by functioning as an oxidase in respiratory protection, with flavodoxin or ferredoxin as the physiological electron donors.

Journal article

Jamshidiha M, Pérez-Dorado I, Murray JW, Tate EW, Cota E, Read RJet al., 2019, Coping with strong translational noncrystallographic symmetry and extreme anisotropy in molecular replacement with Phaser: human Rab27a, Acta Crystallographica Section D Structural Biology, Vol: 75, Pages: 342-353, ISSN: 2059-7983

Data pathologies caused by effects such as diffraction anisotropy and translational noncrystallographic symmetry (tNCS) can dramatically complicate the solution of the crystal structures of macromolecules. Such problems were encountered in determining the structure of a mutant form of Rab27a, a member of the Rab GTPases. Mutant Rab27a constructs that crystallize in the free form were designed for use in the discovery of drugs to reduce primary tumour invasiveness and metastasis. One construct, hRab27a<jats:sup>Mut</jats:sup>, crystallized within 24 h and diffracted to 2.82 Å resolution, with a unit cell possessing room for a large number of protein copies. Initial efforts to solve the structure using molecular replacement by <jats:italic>Phaser</jats:italic> were not successful. Analysis of the data set revealed that the crystals suffered from both extreme anisotropy and strong tNCS. As a result, large numbers of reflections had estimated standard deviations that were much larger than their measured intensities and their expected intensities, revealing problems with the use of such data at the time in <jats:italic>Phaser</jats:italic>. By eliminating extremely weak reflections with the largest combined effects of anisotropy and tNCS, these problems could be avoided, allowing a molecular-replacement solution to be found. The lessons that were learned in solving this structure have guided improvements in the numerical analysis used in <jats:italic>Phaser</jats:italic>, particularly in identifying diffraction measurements that convey very little information content. The calculation of information content could also be applied as an alternative to ellipsoidal truncation. The post-mortem analysis also revealed an oversight in accounting for measurement errors in the fast rotation function. While the crystal of mutant Rab27a is not amenable to drug screening, the structure can guide new modifications to obtain more sui

Journal article

Yu J, Knoppova J, Michoux F, Bialek W, Cota Segura E, Shukla M, Straskova A, Aznar G, Sobotka R, Komenda J, Murray J, Nixon PJet al., 2018, Ycf48 involved in the biogenesis of the oxygen-evolving photosystem II complex is a seven-bladed beta-propeller protein, Proceedings of the National Academy of Sciences, Vol: 115, Pages: E7824-E7833, ISSN: 0027-8424

Robust photosynthesis in chloroplasts and cyanobacteria requires the participation of accessory proteins to facilitate the assembly and maintenance of the photosynthetic apparatus located within the thylakoid membranes. The highly conserved Ycf48 protein acts early in the biogenesis of the oxygen-evolving photosystem II (PSII) complex by binding to newly synthesized precursor D1 subunit and by promoting efficient association with the D2 protein to form a PSII reaction center (PSII RC) assembly intermediate. Ycf48 is also required for efficient replacement of damaged D1 during the repair of PSII. However, the structural features underpinning Ycf48 function remain unclear. Here we show that Ycf48 proteins encoded by the thermophilic cyanobacterium Thermosynechococcus elongatus and the red alga Cyanidioschyzon merolae form seven-bladed beta-propellers with the 19-aa insertion characteristic of eukaryotic Ycf48 located at the junction of blades 3 and 4. Knowledge of these structures has allowed us to identify a conserved “Arg patch” on the surface of Ycf48 that is important for binding of Ycf48 to PSII RCs but also to larger complexes, including trimeric photosystem I (PSI). Reduced accumulation of chlorophyll in the absence of Ycf48 and the association of Ycf48 with PSI provide evidence of a more wide-ranging role for Ycf48 in the biogenesis of the photosynthetic apparatus than previously thought. Copurification of Ycf48 with the cyanobacterial YidC protein insertase supports the involvement of Ycf48 during the cotranslational insertion of chlorophyll-binding apopolypeptides into the membrane.

Journal article

Krysztofinska EM, Evans NJ, Thapaliya A, Murray JW, Morgan RML, Martinez-Lumbreras S, Isaacson RLet al., 2017, Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp., Frontiers in Molecular Biosciences, Vol: 4, ISSN: 2296-889X

Small glutamine-rich tetratricopeptide repeat-containing protein 2 (Sgt2) is a multi-module co-chaperone involved in several protein quality control pathways. The TPR domain of Sgt2 and several other proteins, including SGTA, Hop, and CHIP, is a highly conserved motif known to form transient complexes with molecular chaperones such as Hsp70 and Hsp90. In this work, we present the first high resolution crystal structures of Sgt2_TPR alone and in complex with a C-terminal peptide PTVEEVD from heat shock protein, Ssa1. Using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry, we demonstrate that Sgt2_TPR interacts with peptides corresponding to the C-termini of Ssa1, Hsc82, and Ybr137wp with similar binding modes and affinities.

Journal article

Beckova M, Yu J, Krynicka V, Kozlo A, Shao S, Konik P, Komenda J, Murray JW, Nixon PJet al., 2017, Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria, Philosophical Transactions of the Royal Society B: Biological Sciences, Vol: 372, ISSN: 1471-2970

One strategy for enhancing photosynthesis in crop plants is to improve the ability to repair photosystem II (PSII) in response to irreversible damage by light. Despite the pivotal role of thylakoid embedded FtsH protease complexes in the selective degradation of PSII subunits during repair, little is known about the factors involved in regulating FtsH expression. Here we show using the cyanobacterium Synechocystis sp. PCC 6803 that the Psb29 subunit, originally identified as a minor component of His tagged PSII preparations, physically interacts with FtsH complexes in vivo and is required for normal accumulation of the FtsH2/FtsH3 hetero oligomeric complex involved in PSII repair. We show using X ray crystallography that Psb29 from Thermosynechococcus elongatushas a unique fold consisting of a helical bundle and an extended C terminal helix and contains a highly conserved region that might be involved in binding to FtsH. A similar interaction is likely to occur in Arabidopsis chloroplasts between the Psb29 homologue, termed THF1, and the FTSH2/FTSH5 complex. The direct involvement of Psb29/THF1 in FtsH accumulation helps explain why THF1 is a target during the hypersensitive response in plants induced by pathogen infection. Downregulating FtsH function and the PSII repair cycle via THF1 would contribute to the production

Journal article

Mus F, Eilers BJ, Alleman AB, Kabasakal BV, Wells JN, Murray JW, Nocek BP, DuBois JL, Peters JWet al., 2017, Structural Basis for the Mechanism of ATP-Dependent Acetone Carboxylation, SCIENTIFIC REPORTS, Vol: 7, ISSN: 2045-2322

Microorganisms use carboxylase enzymes to form new carbon-carbon bonds by introducing carbon dioxide gas (CO2) or its hydrated form, bicarbonate (HCO3−), into target molecules. Acetone carboxylases (ACs) catalyze the conversion of substrates acetone and HCO3− to form the product acetoacetate. Many bicarbonate-incorporating carboxylases rely on the organic cofactor biotin for the activation of bicarbonate. ACs contain metal ions but not organic cofactors, and use ATP to activate substrates through phosphorylation. How the enzyme coordinates these phosphorylation events and new C-C bond formation in the absence of biotin has remained a mystery since these enzymes were discovered. The first structural rationale for acetone carboxylation is presented here, focusing on the 360 kDa (αβγ)2 heterohexameric AC from Xanthobacter autotrophicus in the ligand-free, AMP-bound, and acetate coordinated states. These structures suggest successive steps in a catalytic cycle revealing that AC undergoes large conformational changes coupled to substrate activation by ATP to perform C-C bond ligation at a distant Mn center. These results illustrate a new chemical strategy for the conversion of CO2 into biomass, a process of great significance to the global carbon cycle.

Journal article

MacDonald JT, Kabasakal BV, Godding D, Kraatz S, Henderson L, Barber J, Freemont PS, Murray JWet al., 2016, Synthetic beta-solenoid proteins with the fragment-free computational design of a beta-hairpin extension, Proceedings of the National Academy of Sciences of the United States of America, Vol: 113, Pages: 10346-10351, ISSN: 1091-6490

The ability to design and construct structures with atomic level precisionis one of the key goals of nanotechnology. Proteins offer anattractive target for atomic design, as they can be synthesized chemicallyor biologically, and can self-assemble. However the generalizedprotein folding and design problem is unsolved. One approach tosimplifying the problem is to use a repetitive protein as a scaffold.Repeat proteins are intrinsically modular, and their folding and structuresare better understood than large globular domains. Here, wehave developed a new class of synthetic repeat protein, based onthe pentapeptide repeat family of beta-solenoid proteins. We haveconstructed length variants of the basic scaffold, and computationallydesigned de novo loops projecting from the scaffold core. Theexperimentally solved 3.56 ˚A resolution crystal structure of one designedloop matches closely the designed hairpin structure, showingthe computational design of a backbone extension onto a syntheticprotein core without the use of backbone fragments from knownstructures. Two other loop designs were not clearly resolved in thecrystal structures and one loop appeared to be in an incorrect conformation.We have also shown that the repeat unit can accommodatewhole domain insertions by inserting a domain into one of the designedloops.

Journal article

Rutherford AW, Prell J, MacKellar D, Tobin C, Lieber L, Freisen M, Norman JS, Bolger A, Oksaksin M, Chang RL, Ford TL, Nguyen PQ, Woodward J, Permingeat HR, Joshi NS, Silver PA, Usadel B, Murray JWet al., 2016, Streptomyces thermoautotrophicus does not fix nitrogen, Scientific Reports, Vol: 6, ISSN: 2045-2322

Streptomyces thermoautotrophicus UBT1 has been described as a moderately thermophilic chemolithoautotroph with a novel nitrogenase enzyme that is oxygen-insensitive. We have cultured the UBT1 strain, and have isolated two new strains (H1 and P1-2) of very similar phenotypic and genetic characters. These strains show minimal growth on ammonium-free media, and fail to incorporate isotopically labeled N2 gas into biomass in multiple independent assays. The sdn genes previously published as the putative nitrogenase of S. thermoautotrophicus have little similarity to anything found in draft genome sequences, published here, for strains H1 and UBT1, but share >99% nucleotide identity with genes from Hydrogenibacillus schlegelii, a draft genome for which is also presented here. H. schlegelii similarly lacks nitrogenase genes and is a non-diazotroph. We propose reclassification of the species containing strains UBT1, H1, and P1-2 as a non-Streptomycete, non-diazotrophic, facultative chemolithoautotroph and conclude that the existence of the previously proposed oxygen-tolerant nitrogenase is extremely unlikely.

Journal article

Burgess SJ, Hussein T, Yeoman JA, Iamshanova O, Chan KX, Boehm M, Bundy J, Bialek W, Murray JW, Nixon PJet al., 2015, Identification of the elusive pyruvate reductase of Chlamydomonas reinhardtii chloroplasts, Plant and Cell Physiology, Vol: 57, Pages: 82-94, ISSN: 1471-9053

Under anoxic conditions the green alga Chlamydomonas reinhardtii activates various 67 fermentation pathways leading to the creation of formate, acetate, ethanol and small 68 amounts of other metabolites including D-lactate and hydrogen. Progress has been 69 made in identifying the enzymes involved in these pathways and their sub-cellular 70 locations; however, the identity of the enzyme involved in reducing pyruvate to D-71 lactate has remained unclear. Based on sequence comparisons, enzyme activity 72 measurements, X-ray crystallography, biochemical fractionation and analysis of 73 knock-down mutants we conclude that pyruvate reduction in the chloroplast is 74 catalysed by a tetrameric NAD⁺-dependent D-lactate dehydrogenase encoded by 75 Cre07.g324550. Its expression during aerobic growth supports a possible function as a 76 ‘lactate valve’ for the export of lactate to the mitochondrion for oxidation by 77 cytochrome-dependent D-lactate dehydrogenases and by glycolate dehydrogenase. 78 We also present a revised spatial model of fermentation based on our 79 immunochemical detection of the likely pyruvate decarboxylase, PDC3, in the 80 cytoplasm.

Journal article

Cotton CAR, Kabasakal BV, Miah N, Murray JWet al., Structure of the dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase from Thermosynechococcus elongatus bound with sedoheptulose-7-phosphate, Acta Crystallographica Section F, Vol: F71, Pages: 1341-1345, ISSN: 2053-230X

The dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) in cyanobacteria carries out two activities in the Calvin cycle. Structures of this enzyme from the cyanobacterium Synechocystis sp. PCC 6803 exist, but only with adenosine monophosphate (AMP) or fructose-1,6-bisphosphate and AMP bound. The mechanisms which control both selectivity between the two sugars and the structural mechanisms for redox control are still unresolved. Here, the structure of the dual-function FBP/SBPase from the thermophilic cyanobacterium Thermosynechococcus elongatus is presented with sedoheptulose-7-phosphate bound and in the absence of AMP. The structure is globally very similar to the Synechocystis sp. PCC 6803 enzyme, but highlights features of selectivity at the active site and loop ordering at the AMP-binding site. Understanding the selectivity and control of this enzyme is critical for understanding the Calvin cycle in cyanobacteria and for possible biotechnological application in plants.

Journal article

Cotton CA, Douglass JS, De Causmaecker S, Brinkert K, Cardona T, Fantuzzi A, Rutherford AW, Murray JWet al., 2015, Photosynthetic constraints on fuel from microbes., Frontiers in Bioengineering and Biotechnology, Vol: 3, ISSN: 2296-4185

Journal article

Cardona Londono T, Murray JW, Rutherford AW, 2015, Origin and evolution of water oxidation before the last common ancestor of the Cyanobacteria, Molecular Biology and Evolution, ISSN: 1537-1719

Photosystem II, the water oxidizing enzyme, altered the course of evolution by filling the atmosphere with oxygen. Here, we reconstruct the origin and evolution of water oxidation at an unprecedented level of detail by studying the phylogeny of all D1 subunits, the main protein coordinating the water oxidizing cluster (Mn4CaO5) of Photosystem II. We show that D1 exists in several forms making well-defined clades, some of which could have evolved before the origin of water oxidation and presenting many atypical characteristics. The most ancient form is found in the genome of Gloeobacter kilaueensis JS-1 and this has a C-terminus with a higher sequence identity to D2 than to any other D1. Two other groups of early evolving D1 correspond to those expressed under prolonged far-red illumination and in darkness. These atypical D1 forms are characterized by a dramatically different Mn4CaO5 binding site and a Photosystem II containing such a site may assemble an unconventional metal cluster. The first D1 forms with a full set of ligands to the Mn4CaO5 cluster are grouped with D1 proteins expressed only under low oxygen concentrations and the latest evolving form is the dominant type of D1 found in all cyanobacteria and plastids. In addition, we show that the plastid ancestor had a D1 more similar to those in early branching Synechococcus. We suggest each one of these forms of D1 originated from transitional forms at different stages towards the innovation and optimization of water oxidation before the last common ancestor of all known cyanobacteria.

Journal article

Kabasakal BV, Kabasakal BV, Cotton C, Murray JWet al., 2015, Structural insights into malonyl-CoA reductase of 3-hydroxypropionate cycle, Publisher: INT UNION CRYSTALLOGRAPHY, Pages: S202-S202, ISSN: 2053-2733

Conference paper

Hingorani K, Pace R, Whitney S, Murray JW, Smith P, Cheah MH, Wydrzynski T, Hillier Wet al., 2014, Photo-oxidation of tyrosine in a bio-engineered bacterioferritin 'reaction centre'-A protein model for artificial photosynthesis, BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Vol: 1837, Pages: 1821-1834, ISSN: 0005-2728

Journal article

Michoux F, Boehm M, Bialek W, Takasaka K, Maghlaoui K, Barber J, Murray JW, Nixon PJet al., 2014, Crystal structure of CyanoQ from the thermophilic cyanobacterium Thermosynechococcus elongatus and detection in isolated photosystem II complexes, PHOTOSYNTHESIS RESEARCH, Vol: 122, Pages: 57-67, ISSN: 0166-8595

Journal article

Murray JW, 2014, Protein design for artificial photosynthesis, 247th National Spring Meeting of the American-Chemical-Society (ACS), Publisher: AMER CHEMICAL SOC, ISSN: 0065-7727

Conference paper

Bialek W, Wen S, Michoux F, Beckova M, Komenda J, Murray JW, Nixon PJet al., 2013, Crystal structure of the Psb28 accessory factor of Thermosynechococcus elongatus photosystem II at 2.3 angstrom, PHOTOSYNTHESIS RESEARCH, Vol: 117, Pages: 375-383, ISSN: 0166-8595

Journal article

Murray JW, 2013, Light and Life Photosynthesis, Biochemist, Vol: 35, Pages: 4-7, ISSN: 0954-982X

Complex life on Earth requires oxygen as the terminal electron acceptor in the respiratory chain. However, the lifetime of a single oxygen molecule in the atmosphere is only 4500 years. Oxygen is continually being replenished by the action of photosynthetic organisms, using the only substantial energy input to the Earth, sunlight. How this light energy is harvested and used is of fundamental biological importance, and may be of crucial importance in developing sustainable energy technologies. © Biochemical Society.

Journal article

Canning P, Cooper CDO, Krojer T, Murray JW, Pike ACW, Chaikuad A, Keates T, Thangaratnarajah C, Hojzan V, Ayinampudi V, Marsden BD, Gileadi O, Knapp S, von Delft F, Bullock ANet al., 2013, Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases (vol 288, pg 7803, 2013), JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 288, Pages: 28304-28304

Journal article

Moore BL, Kelley LA, Barber J, Murray JW, MacDonald JTet al., 2013, High-quality protein backbone reconstruction from alpha carbons using gaussian mixture models, JOURNAL OF COMPUTATIONAL CHEMISTRY, Vol: 34, Pages: 1881-1889, ISSN: 0192-8651

Journal article

Canning P, Cooper CDO, Krojer T, Murray JW, Pike ACW, Chaikuad A, Keates T, Thangaratnarajah C, Hojzan V, Marsden BD, Gileadi O, Knapp S, von Delft F, Bullock ANet al., 2013, Structural Basis for Cul3 Protein Assembly with the BTB-Kelch Family of E3 Ubiquitin Ligases, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 288, Pages: 7803-7814

Journal article

Simon AC, Simpson PJ, Goldstone RM, Krysztofinska EM, Murray JW, High S, Isaacson RLet al., 2013, Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 110, Pages: 1327-1332, ISSN: 0027-8424

Journal article

Murray J, 2012, Redox active protein maquettes: Multi-functional"green enzymes", RSC Energy and Environment Series, Vol: 2012, Pages: 408-425, ISSN: 2044-0774

Journal article

Murray JW, 2012, Sequence variation at the oxygen-evolving centre of photosystem II: a new class of 'rogue' cyanobacterial D1 proteins, PHOTOSYNTHESIS RESEARCH, Vol: 110, Pages: 177-184, ISSN: 0166-8595

Journal article

Michoux F, Takasaka K, Boehm M, Komenda J, Nixon PJ, Murray JWet al., 2012, Crystal structure of the Psb27 assembly factor at 1.6: implications for binding to Photosystem II, PHOTOSYNTHESIS RESEARCH, Vol: 110, Pages: 169-175, ISSN: 0166-8595

Journal article

Murray JW, 2011, Molecular Solar Fuels, Molecular Solar Fuels, Editors: Wydrzynski, Hillier, Peter, Publisher: RSC, Pages: 408-425, ISBN: 9781849730341

Written by experts, this book presents the latest knowledge and chemical prospects in developing hydrogen as a solar fuel.

Book chapter

Ramboarina S, Garnett JA, Zhou M, Li Y, Peng Z, Taylor JD, Lee W-C, Bodey A, Murray JW, Alguel Y, Bergeron J, Bardiaux B, Sawyer E, Isaacson R, Tagliaferri C, Cota E, Nilges M, Simpson P, Ruiz T, Wu H, Matthews Set al., 2010, Structural Insights into Serine-rich Fimbriae from Gram-positive Bacteria, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 285, Pages: 32446-32457, ISSN: 0021-9258

Journal article

Michoux F, Takasaka K, Boehm M, Nixon PJ, Murray JWet al., 2010, Structure of CyanoP at 2.8 angstrom: Implications for the Evolution and Function of the PsbP Subunit of Photosystem II, BIOCHEMISTRY, Vol: 49, Pages: 7411-7413, ISSN: 0006-2960

Journal article

Eswaran J, Patnaik D, Filippakopoulos P, Wang F, Stein RL, Murray JW, Higgins JMG, Knapp Set al., 2009, Structure and functional characterization of the atypical human kinase haspin, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 106, Pages: 20198-20203, ISSN: 0027-8424

Journal article

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