​

Agirre* J, Atanasova M, Bagdonas H, Ballard CB, Baslé A, Beilsten-Edmands J, Borges RJ, Brown DG, Burgos-Mármol JJ, Berrisford JM, Bond PS, Caballero I, Catapano L, Chojnowski G, Cook AG, Cowtan KD, Croll TI, Debreczeni JÉ, Devenish NE, Dodson EJ, Drevon TR, Emsley P, Evans G, Evans PR, Fando M, Foadi J, Fuentes-Montero L, Garman EF, Gerstel M, Gildea RJ, Hatti K, Hekkelman ML, Heuser P, Hoh SW, Hough MA, Jenkins HT, Jiménez E, Joosten RP, Keegan RM, Keep N, Krissinel EB, Kolenko P, Kovalevskiy O, Lamzin VS, Lawson DM, Lebedev AA, Leslie AGW, Lohkamp B, Long F, Malý M, McCoy AJ, McNicholas SJ, Medina A, Millán C, Murray JW, Murshudov GN, Nicholls RA, Noble MEM, Oeffner R, Pannu NS, Parkhurst JM, Pearce N, Pereira J, Perrakis A, Powell HR, Read RJ, Rigden DJ, Rochira W, Sammito M, Sánchez Rodríguez F, Sheldrick GM, Shelley KL, Simkovic F, Simpkin AJ, Skubak P, Sobolev E, Steiner RA, Stevenson K, Tews I, Thomas JMH, Thorn A, Valls JT, Uski V, Usón I, Vagin A, Velankar S, Vollmar M, Walden H, Waterman D, Wilson KS, Winn MD, Winter G, Wojdyr M, Yamashita K. (2023) The CCP4 suite: integrative software for macromolecular crystallography. Acta Crystallogr D Struct Biol. 79:449-461. doi: 10.1107/S2059798323003595. PMID: 37259835.

​

Steiner* RA (2023) Introduction to the virtual thematic issue on room-temperature biological crystallography. IUCrJ, 10:248-250. doi: 10.1107/S2052252523002968. PMID: 37000491.

(This introduction article was also published in Acta Crystallogr D Struct Biol. (2023) 79:268-270. doi: 10.1107/S2059798323002449. PMID: 37014077 and in Acta Crystallogr F Struct Biol Commun. (2023) 79:79-81. doi: 10.1107/S2053230X23002935. PMID: 37013862.)

​

Zielinski KA, Prester A, Andaleeb H, Bui S, Yefanov O, Catapano L, Henkel A, Wiedorn MO, Lorbeer O, Crosas E, Meyer J, Mariani V, Domaracky M, White TA, Fleckenstein H, Sarrou I, Werner N, Betzel C, Rohde H, Aepfelbacher M, Chapman HN, Perbandt M, Steiner* RA, Oberthuer* D (2022) Rapid and efficient room-temperature serial synchrotron crystallography using the CFEL TapeDrive. IUCrJ, 31:778-791. doi: 10.1107/S2052252522010193. PMID: 36381150.

​

Hight-Warburton W, Felix R, Burton A, Maple H, Chegkazi MS, Steiner RA, McGrath JA, Parsons* M. (2021) α4/α9 integrins coordinate epithelial cell migration through local suppression of MAP kinase signaling pathways. Front Cell Dev Biol 9:750771. doi:10.3389/fcell.2021.750771. PMID: 34900996.

​

Antón Z, Weijman JF, Williams C, Moody ERR, Mantell J, Yip YY, Cross JA, Williams TA, Steiner RA, Crump M, Woolfson DN, Dodding* MP. (2021) Molecular mechanism for kinesin-1 direct membrane recognition. Sci Adv. 7(31):eabg6636. doi: 10.1126/sciadv.abg6636. PMID: 34321209.

​

Cross JA, Chegkazi MS, Steiner* RA, Woolfson* DN, Dodding* MP (2021) A designed high-affinity peptide that hijacks microtubule-based transport. Cell Chem Biol. 28:1347-1355.e5. doi: 10.1016/j.chembiol.2021.03.010. PMID: 33838110.

​

McGregor L, Földes T, Bui S, Moulin M, Coquelle N, Blakeley MP, Rosta E, Steiner* RA (2021) Joint neutron/X-ray crystal structure of a mechanistically relevant complex of perdeuterated urate oxidase and simulations provide insight into the hydration step of catalysis. IUCrJ, 8, 46-59. doi: 10.1107/S2052252520013615. PMID: 33520242.

​

Supsrisunjai C, Hsu CK, Michael M, Duval C, Lee JYW, Yang HS, Huang HY, Chaikul T, Onoufriadis A, Steiner RA, Ariëns RAS, Sarig O, Sprecher E, Eskin-Schwartz M, Samlaska C, Simpson MA, Calonje E, Parsons M, McGrath* JA  (2020) Coagulation Factor XIII-A Subunit Missense Mutation in the Pathobiology of Autosomal Dominant Multiple Dermatofibromas. J Invest Dermatol, 140, 624-635.e7. doi: 10.1016/j.jid.2019.08.441. PMID: 31493396.

​

Pernigo S, Chegkazi MS, Yip YY, Treacy C, Glorani G, Hansen K, Politis A, Bui S, Dodding* MP, Steiner* RA (2018) Structural basis for isoform-specific kinesin-1 recognition by Y-acidic cargo adaptors. eLife Oct 15; 7. pii: e38362. doi: 10.7554/eLife.38362. PMID: 30320553.

​

Randall TS, Yip YY, Wallock-Richards DJ, Pfisterer K, Sanger A, Ficek W, Steiner RA, Beavil AJ, Parsons M, Dodding* MP (2017) A small-molecule activator of kinesin-1 drives remodelling of the microtubule network. Proc Natl Acad Sci USA, 114, 13738-13743. doi: 10.1073/pnas.1715115115. PMID: 29229862.

​

von Stetten* D, Giraud T, Bui S, Steiner RA, Fihman F, de Sanctis* D, Royant* A. (2017) Online Raman spectroscopy for structural biology on beamline ID29 of the ESRF. J Struct Biol, 200, 124-127. doi: 10.1016/j.jsb.2017.10.004. PMID: 29042242.

​

Fin L, Bergamin G, Steiner* RA, Hughes* SM (2017) The Cannabinoid Receptor Interacting Proteins 1 of zebrafish are not required for morphological development, viability or fertility. Sci Rep, 7, 4858. doi: 10.1038/s41598-017-05017-5. PMID: 28687732.

 

Sanger A, Yip YY, Randall TS, Pernigo S, Steiner RA, Dodding* MP (2017) SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. J Cell Sci, 130, 1637-1651. doi: 10.1242/jcs.198267. PMID: 28302907.

​

Steiner* RA, Tucker* JA (2017) Keep it together: restraints in crystallographic refinement of macromolecule-ligand complexes. Acta Crystallogr D73, 93-102. doi: 10.1107/S2059798316017964. PMID: 28177305.

​

Pernigo S, Fukuzawa A, Beedle AE, Holt M, Round A, Pandini A, Garcia-Manyes* S, Gautel* M, Steiner* RA (2017) Binding of Myomesin to Obscurin-Like-1 at the Muscle M-Band Provides a Strategy for Isoform-Specific Mechanical Protection. Structure 25,107-120. doi: 10.1016/j.str.2016.11.015. PMID: 27989621. 

​

Bui S and Steiner* RA (2017) New insight into cofactor-free oxygenation from combined experimental and computational approaches. Curr Opin Struct Biol, 41,109-118. doi: 10.1016/j.sbi.2016.06.015. PMID: 27393973.

​

Twelvetrees AE, Pernigo S, Sanger A, Guedes-Dias P, Schiavo G, Steiner RA, Dodding MP, Holzbaur* EL (2016) The dynamic localization of cytoplasmic dynein in neurons is driven by kinesin-1. Neuron, 90, 1000-1015. doi: 10.1016/j.neuron.2016.04.046. PMID: 27210554.

​

Yip YY, Pernigo S, Sanger A, Xu M, Parsons M, Steiner* RA, Dodding* MP (2016), The light chains of kinesin-1 are autoinhibited. Proc Natl Acad Sci USA, 113, 2418-2423. doi: 10.1073/pnas.1520817113. PMID: 26884162.

​

Santos CX, Hafstad AD, Beretta M, Zhang M, Molenaar C, Kopec J, Fotinou D, Murray TV, Cobb AM, Martin D, Zeh Silva M, Anilkumar N, Schröder K, Shanahan CM, Brewer AC, Brandes RP, Blanc E, Parsons M, Belousov V, Cammack R, Hider RC, Steiner RA, Shah* AM (2016) Targeted redox inhibition of protein phosphatase 1 by Nox4 regulates eIF2α-mediated stress signaling. EMBO J, 35, 319-334. doi: 10.15252/embj.201592394. PMID: 26742780.

​

Hernandez-Ortega A, Quesne MG, Bui S, Heyes DJ, Steiner RA, Scrutton* NS, de Visser* SP (2015) Catalytic mechanism of cofactor-free dioxygenases and how they circumvent spin-forbidden oxygenation of their substrates. J Am Chem Soc, 137, 7474-7487. doi: 10.1021/jacs.5b03836. PMID: 25988744.

​

Pernigo S, Fukuzawa A, Pandini A, Holt M, Kleinjung J, Gautel M, Steiner* RA (2015) The crystal structure of the human titin:obscurin complex reveals a conserved yet specific muscle M-band zipper module. J Mol Biol, 427, 718-736. [Featured Article and Journal Cover]. doi: 10.1016/j.jmb.2014.11.019. PMID: 25490259. 

​

Bui S, von Stetten D, Jambrina PG, Prangé T, Colloc'h N, de Sanctis D, Royant A, Rosta E, Steiner* RA (2014), Direct evidence for a peroxide intermediate and a reactive enzyme-substrate-dioxygen configuration in a cofactor-free oxidase. Angew Chem Int Ed , 53, 13710-13714 [‘Hot Paper’ status]. doi: 10.1002/anie.201405485. PMID: 25314114.

​

Hernandez-Ortega A, Quesne MG, Bui S, Heuts DP, Steiner* RA, Heyes DJ, de Visser SP, Scrutton* NS (2014),Origin of the proton-transfer step in the cofactor-free 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase: effect of the basicity of an active site His residue, J Biol Chem, 289, 8620-8632. doi: 10.1074/jbc.M113.543033. PMID: 24482238.

​

Steiner* RA, "Cu-Dependent Quercetin Dioxygenase" (2013), pp. 1-12 in Encyclopedia of Inorganic and Bioinorganic Chemistry, R.A. Scott ed., John Wiley & Sons Ltd., Chichester, UK. doi: 10.1002/9781119951438.eibc2174. 

​

Pernigo S, Lamprecht A, Steiner* RA, Dodding* MP (2013), Structural basis for kinesin-1:cargo recognition, Science, 340, 356-359. doi: 10.1126/science.1234264. PMID: 23519214.

​

Steiner* RA and Rupp* B (2012), Model building, refinement and validation, Acta Cryst D68, 325-327. (Introduction to the 2011 CCP4 Study Weekend). doi: 10.1107/S0907444912002090. PMID: 22505252.

​

Murshudov* GN, Skubák P, Lebedev AA, Pannu NS, Steiner RA, Nicholls RA, Winn MD, Long F, Vagin AA. (2011) Refmac5 for the refinement of macromolecular structures, Acta Cryst D67, 355-367. doi: 10.1107/S0907444911001314. PMID: 21460454.

​

Schubert HL, Zhai Q, Sandrin V, Eckert DM, Garcia-Maya M, Saul L, Sundquist* WI, Steiner* RA, Hill* CP (2010) Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations, Proc Natl Acad Sci USA, 107, 17951-17956. doi: 10.1073/pnas.1008206107. PMID: 20880831.

​

Fetzner* S. and Steiner* RA (2010) Cofactor-independent oxidases and oxygenases. Appl Microbiol Biotechnol86, 791-804. doi: 10.1007/s00253-010-2455-0. PMID: 20157809. 

​

Pernigo S, Fukuzawa A, Bertz M, Holt M, Rief M, Steiner* RA, Gautel* M (2010) Structural insight into M-band assembly and mechanics from the titin-obscurin-like 1 complex. Proc Natl Acad Sci USA, 107, 2908-2913. doi: 10.1073/pnas.0913736107. PMID: 20133654.

​

Steiner* RA, Janssen HJ, Roversi P, Oakley OJ, Fetzner S (2010) Structural basis for cofactor independent dioxygenation of N-heteroaromatic compounds at the /-hydrolase fold. Proc Natl Acad Sci USA, 107, 657-662. doi: 10.1073/pnas.0909033107. PMID: 20080731. 

​

Steiner* RA, Frerichs-Deeken U, Fetzner S. (2007) Crystallization and preliminary X-ray analysis of 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the / hydrolase fold superfamily. Acta Cryst F63, 382-385. PMID: 17565176. 

​

Valls N, Steiner RA, Wright G, Murshudov GN, Subirana* JA (2005) Variable role of ions in two drug intercalation complexes of DNA. J Biol Inorg Chem 10, 476-482. PMID: 15926069. 

​

Vagin AA, Steiner RA, Lebedev AA, Potterton L, McNicholas S, Long F, Murshudov GN (2004) REFMAC5 dictionary: organization of chemical prior knowledge and guidelines of its use. Acta Cryst D60, 2184-2195. PMID: 15572771.

​

Valls N, Wright, G, Steiner RA, Murshudov GN, Subirana JA (2004) DNA variability in five crystal structures of d(CGCAATTGCG). Acta Cryst D60, 680-685. PMID: 15039556.

​

Steiner RA, Lebedev AA, Murshudov* GN (2003) Fisher’s information in maximum-likelihood crystallographic refinement. Acta Cryst D59, 2114-2124. PMID: 14646069.

​

Fittipaldi M, Steiner RA, Matsushita M, Dijkstra BW, Groenen EJJ, Huber* M. (2003) Single-crystal EPR study at 95 GHz of the type 2 copper site of the inhibitor-bound quercetin 2,3-dioxygenase. Biophys J 85, 4047-4054. PMID: 14645093.

​

Steiner RA, Kalk KH, Dijkstra* BW (2002) Anaerobic enzyme·substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proc Natl Acad Sci USA, 99, 16625-16630. PMID: 12486225. 

​

Steiner RA (2002) Mechanistic studies of the copper-dependent quercetin 2,3-dioxygenase from A. japonicus. X-ray crystallography, spectroscopy and theoretical calculations. Ph.D. thesis. University of Groningen. Print ISBNs 9036715954.

​

Steiner RA, Meyer-Klaucke W, Dijkstra* BW (2002) Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 2. X-ray absorption studies of native enzyme and anaerobic complexes with the substrates quercetin and myricetin. Biochemistry, 41, 7963-7968. PMID: 12069586.

​

Steiner RA, Kooter IM, Dijkstra* BW (2002) Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by X-ray crystallography: inhibition, ordering effect, and mechanistic insights. Biochemistry, 41, 7955-7962. PMID: 12069585.

​

Kooter* IM, Steiner RA, Huber M, Dijkstra BW, van Noort PI, Egmond M (2002) EPR characterization of the mononuclear Cu-containing A. japonicus quercetin 2,3-dioxygenase reveals dramatic changes upon anaerobic binding of substrates. Eur J Biochem 269, 2971-2979. PMID: 12071961.

​

Fusetti F, Schroter KH, Steiner RA, van Noort PI, Pijning T, Rozeboom HJ, Kalk K, Egmond MR, Dijkstra* BW (2002) Crystal structure of the copper-containing quercetin 2,3-dioxygenase from A. japonicus. Structure, 10, 259-268. PMID: 11839311.

​

Steiner RA, Rozeboom HJ, de Vries A, Kalk KH, Murshudov GN, Wilson KS, Dijkstra* BW (2001) X-ray structure of bovine pancreatic phospholipase A2 at atomic resolution. Acta Cryst D57, 516-526. PMID: 11264580.

​

Steiner RA, Murshudov* GN (2000) Flat model bulk solvent correction in the program REFMAC. Acta Cryst A56 (Supplement), s301.

 

Steiner RA, van Noort, PI, Egmond, MR, Dijkstra* BW (2000) Structural basis for the oxygenation of flavonols by quercetin 2,3-dioxygenase. Acta Cryst A56 (Supplement), s77.

​

Wijnen JW, Steiner RA, Engberts* JBFN (1995) 1,3-dipolar cycloaddition of phenyl azide to norbornene in aqueous solutions.

Tetrahedron Lett, 36, 5389-5392.