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OverExpress competent cells citations

Abergel, C., Coutard, B., Byrne, D., Chenivesse, S., Claude, J.-B., Deregnaucourt, C., Fricaux, T., Gianesini-Boutreux, C., Jeudy, S., Lebrun, R., Maza, C., Notredame, C., Poirot, O., Suhre, K., Varagnol, M. and Claverie, J.-M. (2003). Structural genomics of highly conserved microbial genes of unknown function in search of new antibacterial targets. Journal of Structural and Functional Genomics, [online] 4(2-3), pp.141–157. Available at: https://pubmed.ncbi.nlm.nih.gov/14649299/ [Accessed 15 Mar. 2021].

Adams, V., Lucet, I.S., Lyras, D. and Rood, J.I. (2004). DNA binding properties of TnpX indicate that different synapses are formed in the excision and integration of the Tn4451 family. Molecular Microbiology, [online] 53(4), pp.1195–1207. Available at: https://pubmed.ncbi.nlm.nih.gov/15306021/.

Ahn, H.J., Yang, J.K., Lee, B.I., Yoon, H.J., Kim, H.W. and Suh, S.W. (2003). Crystallization and preliminary X-ray crystallographic studies of chorismate synthase from Helicobacter pylori. Acta Crystallographica. Section D, Biological Crystallography, [online] 59(Pt 3), pp.569–571. Available at: https://pubmed.ncbi.nlm.nih.gov/12595729/ [Accessed 15 Mar. 2021].

Albers, S.-V. and Driessen, A.J.M. (2005). Analysis of ATPases of putative secretion operons in the thermoacidophilic archaeon Sulfolobus solfataricus. Microbiology, 151(3), pp.763–773.

Albers, S.-V., Szabó, Z. and Driessen, A.J.M. (2003). Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity. Journal of Bacteriology, [online] 185(13), pp.3918–3925. Available at: https://pubmed.ncbi.nlm.nih.gov/12813086/ [Accessed 15 Mar. 2021].

Alexeyev, M.F., Roberts, R.A.W., Daugherty, R.M., Audia, J.P. and Winkler, H.H. (2004). Cysteine-scanning mutagenesis and thiol modification of the Rickettsia prowazekii ATP/ADP translocase: evidence that transmembrane regions I and II, but not III, are structural components of the aqueous translocation channel. Biochemistry, [online] 43(22), pp.6995–7002. Available at: https://pubmed.ncbi.nlm.nih.gov/15170337/ [Accessed 15 Mar. 2021].

Alexeyev, M.F. and Winkler, H.H. (2002). Complete replacement of basic amino acid residues with cysteines in Rickettsia prowazekii ATP/ADP translocase. Biochimica Et Biophysica Acta, [online] 1565(1), p.136. Available at: https://pubmed.ncbi.nlm.nih.gov/12225862/ [Accessed 15 Mar. 2021].

Allen, M.D., Buckle, A.M., Cordell, S.C., Löwe, J. and Bycroft, M. (2003). The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A. Journal of Molecular Biology, [online] 330(3), pp.503–511. Available at: https://pubmed.ncbi.nlm.nih.gov/12842467/ [Accessed 15 Mar. 2021].

Alonso-CasajúsN., DauvilléeD., Viale, A.M., MuñozF.J., Baroja-FernándezE., Morán-ZorzanoM.T., Eydallin, G., Ball, S. and Pozueta-Romero, J. (2006). Glycogen Phosphorylase, the Product of the glgP Gene, Catalyzes Glycogen Breakdown by Removing Glucose Units from the Nonreducing Ends in Escherichia coli. Journal of Bacteriology, [online] 188(14), pp.5266–5272. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1539952/ [Accessed 15 Mar. 2021].

Anand, S.P., Rajeswari, H., Gupta, P., Srinivasan, R., Indi, S. and Ajitkumar, P. (2004). A C-terminal deletion mutant of Mycobacterium tuberculosis FtsZ shows fast polymerization in vitro. Microbiology, [online] 150(5), pp.1119–1121. Available at: https://pubmed.ncbi.nlm.nih.gov/15133069/ [Accessed 15 Mar. 2021].

Andrade, S.L.A., Dickmanns, A., Ficner, R. and Einsle, O. (2005). Expression, purification and crystallization of the ammonium transporter Amt-1 fromArchaeoglobus fulgidus. Acta Crystallographica Section F Structural Biology and Crystallization Communications, [online] 61(9), pp.861–863. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1978121/ [Accessed 25 May 2019].

Andraos, N., Tabor, S. and Richardson, C.C. (2004). The highly processive DNA polymerase of bacteriophage T5. Role of the unique N and C termini. The Journal of Biological Chemistry, [online] 279(48), pp.50609–50618. Available at: https://pubmed.ncbi.nlm.nih.gov/15377656/ [Accessed 15 Mar. 2021].

Arechaga, I., Butler, P.Jonathan.G. and Walker, J.E. (2002). Self-assembly of ATP synthase subunit c rings. FEBS Letters, 515(1-3), pp.189–193.

Arechaga, I., Miroux, B., Karrasch, S., Huijbregts, R., de Kruijff, B., Runswick, M.J. and Walker, J.E. (2000). Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F(1)F(o) ATP synthase. FEBS letters, [online] 482(3), pp.215–219. Available at: https://pubmed.ncbi.nlm.nih.gov/11024463/ [Accessed 15 Mar. 2021].

Arechaga, I., Miroux, B., Runswick, M.J. and Walker, J.E. (2003). Over-expression ofEscherichia coliF1Fo-ATPase subunit a is inhibited by instability of theuncBgene transcript. FEBS Letters, 547(1-3), pp.97–100.

Banci, L., Bertini, I., Ciurli, S., Dikiy, A., Dittmer, J., Rosato, A., Sciara, G. and Thompsett, A.R. (2002). NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria. Chembiochem: A European Journal of Chemical Biology, [online] 3(4), pp.299–310. Available at: https://pubmed.ncbi.nlm.nih.gov/11933230/ [Accessed 15 Mar. 2021].

Barker, P.D., Bertini, I., Del Conte, R., Ferguson, S.J., Hajieva, P., Tomlinson, E., Turano, P. and Viezzoli, M.S. (2001). A further clue to understanding the mobility of mitochondrial yeast cytochrome c: a (15)N T1rho investigation of the oxidized and reduced species. European Journal of Biochemistry, [online] 268(16), pp.4468–4476. Available at: https://pubmed.ncbi.nlm.nih.gov/11502207/ [Accessed 15 Mar. 2021].

Barrera, F.N., Poveda, J.A., González-Ros, J.M. and Neira, J.L. (2003). Binding of the C-terminal sterile alpha motif (SAM) domain of human p73 to lipid membranes. The Journal of Biological Chemistry, [online] 278(47), pp.46878–46885. Available at: https://pubmed.ncbi.nlm.nih.gov/12954612/ [Accessed 15 Mar. 2021].

Bateman, A. and Bycroft, M. (2000). The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD) 1 1Edited by P. E. Wight. Journal of Molecular Biology, 299(4), pp.1113–1119.

Begum, R.R., Newbold, R.J. and Whitford, D. (2000). Purification of the membrane binding domain of cytochrome b5 by immobilised nickel chelate chromatography. Journal of Chromatography. B, Biomedical Sciences and Applications, [online] 737(1-2), pp.119–130. Available at: https://pubmed.ncbi.nlm.nih.gov/10681048/ [Accessed 15 Mar. 2021].

Belogurov, G.A. and Lahti, R. (2002). A lysine substitute for K+. A460K mutation eliminates K+ dependence in H+-pyrophosphatase of Carboxydothermus hydrogenoformans. The Journal of Biological Chemistry, [online] 277(51), pp.49651–49654. Available at: https://pubmed.ncbi.nlm.nih.gov/12401795/ [Accessed 15 Mar. 2021].

Belogurov, G.A., Malinen, A.M., Turkina, M.V., Jalonen, U., Rytkönen, K., Baykov, A.A. and Lahti, R. (2005). Membrane-bound pyrophosphatase of Thermotoga maritima requires sodium for activity. Biochemistry, [online] 44(6), pp.2088–2096. Available at: https://pubmed.ncbi.nlm.nih.gov/15697234/ [Accessed 15 Mar. 2021].

Belogurov, G.A., Turkina, M.V., Penttinen, A., Huopalahti, S., Baykov, A.A. and Lahti, R. (2002). H+-pyrophosphatase of Rhodospirillum rubrum. High yield expression in Escherichia coli and identification of the Cys residues responsible for inactivation my mersalyl. The Journal of Biological Chemistry, [online] 277(25), pp.22209–22214. Available at: https://pubmed.ncbi.nlm.nih.gov/11956221/ [Accessed 15 Mar. 2021].

Bernard, R., El Ghachi, M., Mengin-Lecreulx, D., Chippaux, M. and Denizot, F. (2005). BcrC from Bacillus subtilis acts as an undecaprenyl pyrophosphate phosphatase in bacitracin resistance. The Journal of Biological Chemistry, [online] 280(32), pp.28852–28857. Available at: https://pubmed.ncbi.nlm.nih.gov/15946938/ [Accessed 15 Mar. 2021].

Berthold, D.A., Stenmark, P. and Nordlund, P. (2003). Screening for functional expression and overexpression of a family of diiron-containing interfacial membrane proteins using the univector recombination system. Protein Science: A Publication of the Protein Society, [online] 12(1), pp.124–134. Available at: https://pubmed.ncbi.nlm.nih.gov/12493835/ [Accessed 15 Mar. 2021].

Berthold, D.A., Voevodskaya, N., Stenmark, P., Gräslund, A. and Nordlund, P. (2002). EPR studies of the mitochondrial alternative oxidase. Evidence for a diiron carboxylate center. The Journal of Biological Chemistry, [online] 277(46), pp.43608–43614. Available at: https://pubmed.ncbi.nlm.nih.gov/12215444/ [Accessed 15 Mar. 2021].

Besche, H., Tamura, N., Tamura, T. and Zwickl, P. (2004). Mutational analysis of conserved AAA+ residues in the archaeal Lon protease from Thermoplasma acidophilum. FEBS letters, [online] 574(1-3), pp.161–166. Available at: https://pubmed.ncbi.nlm.nih.gov/15358558/ [Accessed 15 Mar. 2021].

Besche, H. and Zwickl, P. (2004). The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active site. European Journal of Biochemistry, [online] 271(22), pp.4361–4365. Available at: https://pubmed.ncbi.nlm.nih.gov/15560777/ [Accessed 15 Mar. 2021].

Best, R.B., Li, B., Steward, A., Daggett, V. and Clarke, J. (2001). Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophysical Journal, [online] 81(4), pp.2344–2356. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1301705/ [Accessed 15 Mar. 2021].

BLAKEY, D., LEECH, A., THOMAS, G.H., COUTTS, G., FINDLAY, K. and MERRICK, M. (2002). Purification of the Escherichia coli ammonium transporter AmtB reveals a trimeric stoichiometry. Biochemical Journal, 364(2), pp.527–535.

Bolam, D.N., Xie, H., Pell, G., Hogg, D., Galbraith, G., Henrissat, B. and Gilbert, H.J. (2004). X4 modules represent a new family of carbohydrate-binding modules that display novel properties. The Journal of Biological Chemistry, [online] 279(22), pp.22953–22963. Available at: https://pubmed.ncbi.nlm.nih.gov/15004012/ [Accessed 15 Mar. 2021].

Bonomo, J. and Gill, R.T. (2005). Amino acid content of recombinant proteins influences the metabolic burden response. Biotechnology and Bioengineering, [online] 90(1), pp.116–126. Available at: https://pubmed.ncbi.nlm.nih.gov/15736162/ [Accessed 15 Mar. 2021].

Borges-Walmsley, M.I., Beauchamp, J., Kelly, S.M., Jumel, K., Candlish, D., Harding, S.E., Price, N.C. and Walmsley, A.R. (2003). Identification of Oligomerization and Drug-binding Domains of the Membrane Fusion Protein EmrA. Journal of Biological Chemistry, [online] 278(15), pp.12903–12912. Available at: https://www.jbc.org/content/278/15/12903 [Accessed 6 Nov. 2020].

Borges-Walmsley, M.I., Du, D., McKeegan, K.S., Sharples, G.J. and Walmsley, A.R. (2005). VceR Regulates the vceCAB Drug Efflux Pump Operon of Vibrio cholerae by Alternating Between Mutually Exclusive Conformations that Bind either Drugs or Promoter DNA. Journal of Molecular Biology, 349(2), pp.387–400.

Bossing, T. and Brand, A.H. (2002). Dephrin, a transmembrane ephrin with a unique structure, prevents interneuronal axons from exiting the Drosophila embryonic CNS. Development, [online] 129(18), pp.4205–4218. Available at: https://dev.biologists.org/content/129/18/4205 [Accessed 15 Mar. 2021].

Bouckaert, J., Berglund, J., Schembri, M., De Genst, E., Cools, L., Wuhrer, M., Hung, C.-S., Pinkner, J., Slättegård, R., Zavialov, A., Choudhury, D., Langermann, S., Hultgren, S.J., Wyns, L., Klemm, P., Oscarson, S., Knight, S.D. and De Greve, H. (2005). Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin. Molecular Microbiology, [online] 55(2), pp.441–455. Available at: https://pubmed.ncbi.nlm.nih.gov/15659162/ [Accessed 15 Mar. 2021].

Bouhss, A., Crouvoisier, M., Blanot, D. and Mengin-Lecreulx, D. (2004). Purification and characterization of the bacterial MraY translocase catalyzing the first membrane step of peptidoglycan biosynthesis. The Journal of Biological Chemistry, [online] 279(29), pp.29974–29980. Available at: https://pubmed.ncbi.nlm.nih.gov/15131133/ [Accessed 15 Mar. 2021].

Bourhis, J.-M., Receveur-Bréchot, V., Oglesbee, M., Zhang, X., Buccellato, M., Darbon, H., Canard, B., Finet, S. and Longhi, S. (2005). The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. Protein Science, 14(8), pp.1975–1992.

Bravo, J., Karathanassis, D., Pacold, C.M., Pacold, M.E., Ellson, C.D., Anderson, K.E., Butler, P.J.G., Lavenir, I., Perisic, O., Hawkins, P.T., Stephens, L. and Williams, R.L. (2001). The Crystal Structure of the PX Domain from p40phox Bound to Phosphatidylinositol 3-Phosphate. Molecular Cell, [online] 8(4), pp.829–839. Available at: https://www.cell.com/fulltext/S1097-2765(01)00372-0 [Accessed 15 Mar. 2021].

Broutin, I., Benabdelhak, H., Moreel, X., Lascombe, M.-B., Lerouge, D. and Ducruix, A. (2005). Expression, purification, crystallization and preliminary X-ray studies of the outer membrane efflux proteins OprM and OprN from Pseudomonas aeruginosa. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, [online] 61(Pt 3), pp.315–318. Available at: https://pubmed.ncbi.nlm.nih.gov/16511029/ [Accessed 15 Mar. 2021].

Brown, A.K., Sridharan, S., Kremer, L., Lindenberg, S., Dover, L.G., Sacchettini, J.C. and Besra, G.S. (2005). Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity. The Journal of Biological Chemistry, [online] 280(37), pp.32539–32547. Available at: https://pubmed.ncbi.nlm.nih.gov/16040614/ [Accessed 15 Mar. 2021].

Buchberger, Howard, Freund, Proctor, Butler, Fersht and Bycroft (2000). Biophysical characterization of elongin C from saccharomyces cerevisiae. Biochemistry, [online] 39(40), p.12512. Available at: https://pubmed.ncbi.nlm.nih.gov/11015233/ [Accessed 15 Mar. 2021].

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Cabezon, E., Butler, P.J.G., Runswick, M.J. and Walker, J.E. (2000). Modulation of the Oligomerization State of the Bovine F1-ATPase Inhibitor Protein, IF1, by pH. Journal of Biological Chemistry, 275(33), pp.25460–25464.

Caldovic, L., Morizono, H., Panglao, M.G., Lopez, G.Y., Shi, D., Summar, M.L. and Tuchman, M. (2005). Late onset N-acetylglutamate synthase deficiency caused by hypomorphic alleles. Human Mutation, [online] 25(3), pp.293–298. Available at: https://pubmed.ncbi.nlm.nih.gov/15714518/ [Accessed 15 Mar. 2021].

Campanacci, V., Egloff, M.-P., Longhi, S., Ferron, F., Rancurel, C., Salomoni, A., Durousseau, C., Tocque, F., Brémond, N., Dobbe, J.C., Snijder, E.J., Canard, B. and Cambillau, C. (2003). Structural genomics of the SARS coronavirus: cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein. Acta Crystallographica. Section D, Biological Crystallography, [online] 59(Pt 9), pp.1628–1631. Available at: https://pubmed.ncbi.nlm.nih.gov/12925794/ [Accessed 15 Mar. 2021].

Cannon, K.S., Or, E., Clemons, W.M., Shibata, Y. and Rapoport, T.A. (2005). Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. The Journal of Cell Biology, [online] 169(2), pp.219–225. Available at: https://pubmed.ncbi.nlm.nih.gov/15851514/ [Accessed 15 Mar. 2021].

Carbajo, R.J., Kellas, F.A., Runswick, M.J., Montgomery, M.G., Walker, J.E. and Neuhaus, D. (2005). Structure of the F1-binding Domain of the Stator of Bovine F1Fo-ATPase and How it Binds an α-Subunit. Journal of Molecular Biology, [online] 351(4), pp.824–838. Available at: https://www.sciencedirect.com/science/article/abs/pii/S0022283605006625 [Accessed 15 Mar. 2021].

Carbajo, R.J., Silvester, J.A., Runswick, M.J., Walker, J.E. and Neuhaus, D. (2004). Solution Structure of Subunit F6 from the Peripheral Stalk Region of ATP Synthase from Bovine Heart Mitochondria. Journal of Molecular Biology, 342(2), pp.593–603.

Carrion-Vazquez, M., Oberhauser, A.F., Fowler, S.B., Marszalek, P.E., Broedel, S.E., Clarke, J. and Fernandez, J.M. (1999). Mechanical and chemical unfolding of a single protein: A comparison. Proceedings of the National Academy of Sciences, [online] 96(7), pp.3694–3699. Available at: https://www.pnas.org/content/96/7/3694 [Accessed 15 Mar. 2021].

Chami, M., Steinfels, E., Orelle, C., Jault, J.-M., Di Pietro, A., Rigaud, J.-L. and Marco, S. (2002). Three-dimensional structure by cryo-electron microscopy of YvcC, an homodimeric ATP-binding cassette transporter from Bacillus subtilis. Journal of Molecular Biology, [online] 315(5), pp.1075–1085. Available at: https://pubmed.ncbi.nlm.nih.gov/11827477/ [Accessed 15 Mar. 2021].

Chan, H.Y.E., Brogna, S. and O’Kane, C.J. (2001). Dribble, the Drosophila KRR1p Homologue, Is Involved in rRNA Processing. Molecular Biology of the Cell, 12(5), pp.1409–1419.

Chaney, M., Grande, R., Wigneshweraraj, S.R., Cannon, W., Casaz, P., Gallegos, M.T., Schumacher, J., Jones, S., Elderkin, S., Dago, A.E., Morett, E. and Buck, M. (2001). Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP-aluminum fluoride: insights into activator mechanochemical action. Genes & Development, [online] 15(17), pp.2282–2294. Available at: https://pubmed.ncbi.nlm.nih.gov/11544185/ [Accessed 15 Mar. 2021].

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Chen, Y.W., Allen, M.D., Veprintsev, D.B., Löwe, J. and Bycroft, M. (2004). The Structure of the AXH Domain of Spinocerebellar Ataxin-1. Journal of Biological Chemistry, 279(5), pp.3758–3765.

Cheng, D., Kelley, R.W., Cawley, G.F. and Backes, W.L. (2004). High-level expression of recombinant rabbit cytochrome P450 2E1 in Escherichia coli C41 and its purification. Protein Expression and Purification, [online] 33(1), pp.66–71. Available at: https://pubmed.ncbi.nlm.nih.gov/14680963/ [Accessed 15 Mar. 2021].

Cheung, C.P., Yu, S., Wong, K.B., Chan, L.W., Lai, F.M.M., Wang, X., Suetsugi, M., Chen, S. and Chan, F.L. (2005). Expression and functional study of estrogen receptor-related receptors in human prostatic cells and tissues. The Journal of Clinical Endocrinology and Metabolism, [online] 90(3), pp.1830–1844. Available at: https://pubmed.ncbi.nlm.nih.gov/15598686/ [Accessed 15 Mar. 2021].

Cheung, J.K., Dupuy, B., Deveson, D.S. and Rood, J.I. (2004a). The Spatial Organization of the VirR Boxes Is Critical for VirR-Mediated Expression of the Perfringolysin O Gene, pfoA, from Clostridium perfringens. Journal of Bacteriology, 186(11), pp.3321–3330.

Cheung, Y.-Y., Allen, M.D., Bycroft, M. and Wong, K.-B. (2004b). Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeonPyrococcus horikoshii. Acta Crystallographica Section D Biological Crystallography, 60(7), pp.1308–1310.

Christ, D. and Winter, G. (2003). Identification of functional similarities between proteins using directed evolution. Proceedings of the National Academy of Sciences, 100(23), pp.13202–13206.

Clabecq, A., Henry, J.P. and Darchen, F. (2000). Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP. The Journal of Biological Chemistry, [online] 275(41), pp.31786–31791. Available at: https://pubmed.ncbi.nlm.nih.gov/10859313/.

Claret, L., Calder, S.R., Higgins, M. and Hughes, C. (2003). Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly. Molecular microbiology, [online] 48(5), pp.1349–55. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2528289/ [Accessed 23 Sep. 2019].

Clarke, T.A., Im, S.-C., Bidwai, A. and Waskell, L. (2004). The role of the length and sequence of the linker domain of cytochrome b5 in stimulating cytochrome P450 2B4 catalysis. The Journal of Biological Chemistry, [online] 279(35), pp.36809–36818. Available at: https://pubmed.ncbi.nlm.nih.gov/15194706/ [Accessed 15 Mar. 2021].

Clayton, G.M., Peak-Chew, S.Y., Evans, R.M. and Schwabe, J.W.R. (2001). The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation. Proceedings of the National Academy of Sciences, [online] 98(4), pp.1549–1554. Available at: https://www.pnas.org/content/98/4/1549 [Accessed 15 Mar. 2021].

Cohen, H.M., Tawfik, D.S. and Griffiths, A.D. (2002). Promiscuous methylation of non-canonical DNA sites by HaeIII methyltransferase. Nucleic Acids Research, [online] 30(17), pp.3880–3885. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC137429/ [Accessed 15 Mar. 2021].

Collinson, I., Breyton, C., Duong, F., Tziatzios, C., Schubert, D., Or, E., Rapoport, T. and Kühlbrandt, W. (2001). Projection structure and oligomeric properties of a bacterial core protein translocase. The EMBO Journal, [online] 20(10), pp.2462–2471. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC125464/ [Accessed 15 Mar. 2021].

Crystal structure of the bacterial cell division regulator MinD. (2001). FEBS Letters, [online] 492(1-2), pp.160–165. Available at: https://www.sciencedirect.com/science/article/pii/S0014579301022165 [Accessed 15 Mar. 2021].

Rodríguez, A.Chapin. and Stock, D. (2002). Crystal structure of reverse gyrase: insights into the positive supercoiling of DNA. The EMBO Journal, 21(3), pp.418–426.

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