• Susa KJ, Rawson S, Kruse AC*, Blacklow SC*. Cryo-EM structure of the B cell co-receptor CD19 bound to the tetraspanin CD81. (2021) Science 371, 300-305. *Corresponding authors.
  • Amcheslavsky A, Wallace AL, Ejemel M, Li Q, McMahon CT, Stoppato M, Giuntini S, Schiller ZA, Pondish JR, Toomey JR, Schneider RM, Meisinger J, Heukers R, Kruse AC, Barry EM, Pierce BG, Klempner MS, Cavacini LA, Wang Y. Anti-CfaE nanobodies provide broad cross-protection against major pathogenic enterotoxigenic Escherichia coli strains, with implications for vaccine design. (2021) Sci. Rep. 11, 2751.
  • Skiba MA, Kruse AC. Autoantibodies as Endogenous Modulators of GPCR Signaling. (2021) Trends. Pharmacol. Sci. 42, 135-150.


  • Susa KJ, Seegar TC, Blacklow SC*, Kruse AC*. A dynamic interaction between CD19 and the tetraspanin CD81 controls B cell co-receptor trafficking. (2020) eLife, 9:e52337. *Corresponding authors.
  • Sjodt M, Rohs PDA, Gilman MSA, Erlandson SC, Zheng S, Green AG, Brock KP, Taguchi A, Kahne D, Walker S, Marks DS, Rudner DZ, Bernhardt TG, Kruse AC. Structural coordination of polymerization and crosslinking by a SEDS-bPBP peptidoglycan synthase complex. (2020) Nat. Microbiol., 5, 813-820.
  • Yu C, Wang L, Rowe RG, Han A, Ji W, McMahon C, Baier AS, Huang YC, Marion W, Pearson DS, Kruse AC, Daley GQ, Wu H, Sliz P. A nanobody targeting the LIN28:let-7 interaction fragment of TUT4 blocks uridylation of let-7. (2020) Proc. Natl. Acad. Sci. U. S. A. 117, 4653-4663.
  • Suomivuori CM, Lotorraca NR, Wingler LM, Eismann S, King MC, Kleinhenz ALW, Skiba MA, Staus DP, Kruse AC, Lefkowitz RJ, Dror RO. Molecular mechanism of biased signaling in a prototypical G protein-coupled receptor. (2020) Science 367, 881-887.
  • Wingler LM, Skiba MA, McMahon C, Staus DP, Kleinhenz LW, Suomivuori CM, Latorraca NR, Dror RO, Lefkowitz RJ*, Kruse AC*. Angiotensin and biased analogs induce structurally distinct active conformations within a GPCR. (2020) Science 367, 888-892. *Corresponding authors.
  • Pascolutti R, Erlandson SC, Burri DJ, Zheng S, Kruse AC. Mapping and engineering the interaction between adiponectin and T-cadherin. (2020) J. Biol. Chem. 295, 2749-2759.


  • Schmidt HR, Kruse AC. The molecular function of sigma receptors: past, present, and future. (2019) Trends Pharmacol. Sci. 40, 636-654.
  • Chen H, Nwe P, Yang Y, Rosen CE, Bielecka AA, Kuchroo M, Cline GW, Kruse AC, Ring AM, Crawford JM, Palm NW. A forward chemical genetic screen reveals gut microbiota metabolites that modulate host physiology. (2019) Cell 177, 1217-1231.
  • Owens T, Taylor R, Pahil K, Bertani B, Ruiz N*, Kruse AC*, Kahne D*. Structural basis for unidirectional export of lipopolysaccharide to the cell surface. (2019) Nature 567, 550-553. *Corresponding authors
  • Zheng S, Abreu N, Levitz J, Kruse AC. Structural basis for KCTD-mediated rapid desensitization of GABA-B signaling. (2019) Nature 567, 127-131.
  • Taguchi A, Welsh MA, Marmont LS, Lee W, Sjodt M, Kruse AC, Kahne D, Bernhardt TG, Walker S. FtsW is a peptidoglycan polymerase that is functional only in complex with its cognate penicillin-binding protein. (2019) Nat. Microbiol. 4, 587-594.
  • Zheng S, Kruse AC. Solving a specificity mystery. (2019) eLife e44298. (Commentary)
  • Wingler LM*, McMahon C*, Staus DP*, Lefkowitz RJ, Kruse AC. Structure of active-state angiotensin receptor stabilized by a synthetic nanobody. (2019) Cell 76, 479-490. *Equal contributors


  • Ramírez-Guadiana FH, Rodrigues CDA, Marquis KA, Campo N, Barajas-Ornelas R, Brock K, Marks DS, Kruse AC, Rudner DZ. Evidence that regulation of intramembrane proteolysis is mediated by substrate gating during sporulation in Bacillus subtilis. (2018) PLoS Genet. 14(11):e1007753
  • Rohs PDA, Buss J, Sim SI, Squyres GR, Srisuknimit V, Smith M, Cho H, Sjodt M, Kruse AC, Garner EC, Walker S, Kahne DE, Bernhardt TG. A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery. (2018) PLoS Genet. 14(10):e1007726.
  • Schmidt HR, Betz RM, Dror RO, Kruse AC. Structural basis for σ1 receptor ligand recognition. (2018) Nat. Struct. Mol. Biol. 25, 981-987.
  • Wang X, Hughes AC, Brandão HB, Walker B, Lierz C, Cochran JC, Oakley MG, Kruse AC, Rudner DZ. In Vivo Evidence for ATPase-Dependent DNA Translocation by the Bacillus subtilis SMC Condensin Complex. (2018) Mol. Cell S1097-2765(18)30553-7
  • Sham LT, Zheng S, Yakhnina AA, Kruse AC, Bernhardt TG. Loss of specificity variants of WzxC suggest that substrate recognition is coupled with transporter opening in MOP-family flippases. (2018) Mol. Microbiol. 109, 633-641.
  • Zheng S, Sham LT, Rubino FA, Brock KP, Robins WP, Mekalanos JJ, Marks DS, Bernhardt TG, Kruse AC. Structure and mutagenic analysis of the lipid II flippase MurJ from Escherichia coli. (2018) Proc. Natl. Acad. Sci. U.S.A. 115, 6709-6714.
  • Huang P, Zheng S, Wierbowski BM, Kim Y, Nedelcu D, Aravena L, Liu J, Kruse AC, Salic A. Structural Basis of Smoothened Activation in Hedgehog Signaling. (2018) Cell. 174, 312-324.
  • Linkens K, Schmidt HR, Sahn JJ, Kruse AC, Martin SF. Investigating isoindoline, tetrahydroisoquinoline, and tetrahydrobenzazepine scaffolds for their sigma receptor binding properties. (2018) Eur. J. Med. Chem. 151, 557-567.
  • Sjodt M, Brock K, Dobihal G, Rohs PDA, Green AG, Hopf TA, Meeske AJ, Srisuknimit V, Kahne D, Walker S, Marks DS, Bernhardt TG, Rudner DZ, Kruse AC. Structure of the peptidoglycan polymerase RodA resolved by evolutionary coupling analysis. (2018) Nature 556, 118-121.
  • Staus DP, Wingler LM, Choi M, Pani B, Manglik A, Kruse AC, Lefkowitz RJ. Sortase ligation enables homogeneous GPCR phosphorylation to reveal diversity in β-arrestin coupling. (2018) Proc. Natl. Acad. Sci. U.S.A. 115, 3834-3839.
  • Erlandson SC, McMahon C, Kruse AC. Structural Basis for G Protein-Coupled Receptor Signaling. (2018) Annu. Rev. Biophys. Epub ahead of print.
  • Korczynska M, Clark MJ, Valant C, Xu J, Moo EV, Albold S, Weiss DR, Torosyan H, Huang W, Kruse AC, Lyda BR, May LT, Baltos JA, Sexton PM, Kobilka BK, Christopoulos A, Shoichet BK, Sunahara RK. Structure-based discovery of selective positive allosteric modulators of antagonists for the M2 muscarinic acetylcholine receptor. (2018) Proc. Natl. Acad. Sci. U.S.A. 6;115(10):E2419-E2428.
  • McMahon C, Baier AS, Pascolutti R, Wegrecki M, Zheng S, Ong JX, Erlandson SC, Hilger D, Rasmussen SGF, Ring AM, Manglik A*, Kruse AC*. Yeast surface display platform for rapid discovery of conformationally selective nanobodies. (2018) Nat. Struct. Mol. Biol. 25(3):289-296. *Corresponding authors


  • Seegar TCM, Killingsworth LB, Saha N, Meyer PA, Patra D, Zimmerman B, Janes PW, Rubinstein E, Nikolov DB, Skiniotis G, Kruse AC, Blacklow SC. Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10. (2017) Cell 171, 1638-1648.
  • Manglik A*, Kruse AC*. Structural basis for G protein-coupled receptor activation. (2017) Biochemistry. Online ahead of print. *Co-corresponding.
  • Ramírez-Guadiana FH, Meeske AJ, Rodrigues CDA, Barajas-Ornelas RDC, Kruse AC, Rudner DZ. A two-step transport pathway allows the mother cell to nurture the developing spore in Bacillus subtilis. (2017) PLoS Genet. 13, e1007015.
  • Alon A*, Schmidt HR*, Wood MD*, Sahn JJ, Martin SF, Kruse AC. Identification of the gene that codes for the sigma-2 receptor. (2017) Proc. Natl. Acad. Sci. U.S.A. 114, 7160-7165. *Equal contributors
  • Sguazzini E, Schmidt HR, Iyer KA, Kruse AC, Dukat M. Reevaluation of fenpropimorph as a sigma receptor ligand: Structure-affinity relationship studies at human sigma-1 receptors. (2017) Bioorg. Med. Chem. Lett. 27, 2912-2919.
  • Paek J*, Kalocsay M*, Staus DP, Wingler L, Pascolutti R, Paulo JA, Gygi SP, Kruse AC. Multidimensional tracking of GPCR signaling via peroxidase-catalyzed proximity labeling. (2017) Cell 169, 338-349. *Equal contributors.
  • Alon A, Schmidt HR, Zheng S, Kruse AC. Structural Perspectives on sigma-1 receptor function. (2017) in Sylvia Smith et al. (Eds.), Sigma Receptors: Their Role in Disease and as Therapeutic Targets. Adv. Exp. Med. Biol., Vol. 964.
  • Kruse AC. (2017) Structural insights into sigma1 function. Handb. Exp. Pharmacol.


  • Zimmerman B, Kelly B, McMillan BJ, Seegar TCM, Dror RO, Kruse AC*, Blacklow SC*. Crystal structure of a full-length human tetraspanin reveals a cholesterol binding pocket. (2016) Cell 167, 1041-1051. *Co-corresponding
  • Pascolutti R, Sun X, Kao J, Maute RL, Ring AM, Bowman GR, Kruse AC. Structure and dynamics of PD-L1 and an ultra high-affinity PD-1 receptor mutant. (2016) Structure 24, 1719-1728.
  • Meeske AJ, Riley EP, Robins WP, Uehara T, Mekalanos JJ, Kahne D, Walker S, Kruse AC, Bernhardt TG, Rudner DZ. SEDS proteins are a widespread family of bacterial cell wall polymerases. (2016) Nature 537, 634-638.
  • Staus DP, Strachan RT, Manglik A, Pani B, Kahsai AW, Kim TH, Wingler LM, Ahn S, Chatterjee A, Masoudi A, Kruse AC, Pardon E, Steyaert J, Weis WI, Prosser RS, Kobilka BK, Costa T, Lefkowitz RJ. Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation. (2016) Nature 535, 448-452.
  • Schmidt HR*, Zheng S*, Gurpinar E, Koehl A, Manglik A, Kruse AC. Crystal structure of the human sigma-1 receptor (2016) Nature 532, 527-530. *Equal contributors
  • Meyer PA, Socias S, Key J, Ransey E, Tjon EC, Buschiazzo A, Lei M, Botka C, Withrow J, Neau D, Rajashankar K, Anderson KS, Baxter RH, Blacklow SC, Boggon TJ, Bonvin AM, Borek D, Brett TJ, Caflisch A, Chang CI, Chazin WJ, Corbett KD, Cosgrove MS, Crosson S, Dhe-Paganon S, Di Cera E, Drennan CL, Eck MJ, Eichman BF, Fan QR, Ferré-D'Amaré AR, Christopher Fromme J, Garcia KC, Gaudet R, Gong P, Harrison SC, Heldwein EE, Jia Z, Keenan RJ, Kruse AC, Kvansakul M, McLellan JS, Modis Y, Nam Y, Otwinowski Z, Pai EF, Pereira PJ, Petosa C, Raman CS, Rapoport TA, Roll-Mecak A, Rosen MK, Rudenko G, Schlessinger J, Schwartz TU, Shamoo Y, Sondermann H, Tao YJ, Tolia NH, Tsodikov OV, Westover KD, Wu H, Foster I, Fraser JS, Maia FR, Gonen T, Kirchhausen T, Diederichs K, Crosas M, Sliz P. Data publication with the structural biology data grid supports live analysis. (2016) Nat. Commun. 7, 10882
  • Baxter EL, Aguila L, Alonso-Mori R, Barnes CO, Bonagura CA, Brehmer W, Brunger AT, Calero G, Caradoc-Davies TT, Chatterjee R, Degrado WF, Fraser JS, Ibrahim M, Kern J, Kobilka BK, Kruse AC, Larsson KM, Lemke HT, Lyubimov AY, Manglik A, McPhillips SE, Norgren E, Pang SS, Soltis SM, Song J, Thomaston J, Tsai Y, Weis WI, Woldeyes RA, Yachandra V, Yano J, Zouni A, Cohen AE. High-density grids for efficient data collection from multiple crystals. (2016) Acta Crystallogr. D72, 2-11.


  • Li Q, Tachie-Baffour Y, Liu Z, Baldwin MW, Kruse AC, Liberles SD. Non-classical amine recognition evolved in a large clade of olfactory receptors. (2015) eLife, 4:e10441.
  • Maute RL, Gordon SR, Mayer AT, McCracken MN, Natarajan A, Ring NG, Kimura R, Tsai JM, Manglik A, Kruse AC, Gambhir SS, Weissman IL, Ring AM. Engineering high-affinity PD-1 variants for optimized immunotherapy and immune-PET imaging. (2015) Proc. Natl. Acad. Sci. USA, 112, E6506-E6514.


  • Cohen AE, Soltis SM, González A, Aguila L, Alonso-Mori R, Barnes CO, Baxter EL, Brehmer W, Brewster AS, Brunger AT, Calero G, Chang JF, Chollet M, Ehrensberger P, Eriksson TL, Feng Y, Hattne J, Hedman B, Hollenbeck M, Holton JM, Keable S, Kobilka BK, Kovaleva EG, Kruse AC, Lemke HT, Lin G, Lyubimov AY, Manglik A, Mathews II, McPhillips SE, Nelson S, Peters JW, Sauter NK, Smith CA, Song J, Stevenson HP, Tsai Y, Uervirojnangkoorn M, Vinetsky V, Wakatsuki S, Weis WI, Zadvornyy OA, Zeldin OB, Zhu D, Hodgson KO. Goniometer-based femtosecond crystallography with X-ray free electron lasers. (2014) Proc. Natl. Acad. Sci. USA, 111, 17122-17127.
  • Kruse AC, Kobilka BK, Gautam D, Sexton PM, Christopoulos A, Wess J. Muscarinic acetylcholine receptors: novel opportunities for drug development. (2014) Nat. Rev. Drug Discov., 13, 549-560.
  • Kruse AC*, Hu J, Kobilka BK, Wess J*. Muscarinic acetylcholine receptor X-ray structures: potential implications for drug development. (2014) Curr. Opin. Pharmacol. 16C, 24-30. *Corresponding
  • Weichert D, Kruse AC, Manglik A, Hiller C, Zhang C, Hübner H, Kobilka BK, Gmeiner P. Covalent neurotransmitter surrogates for the structural investigation of aminergic G protein-coupled receptors. (2014) Proc. Natl. Acad. Sci. USA 111, 10744-10748.


  • Kruse AC*, Ring AM*, Manglik A, Hu J, Hu K, Eitel K, Hübner H, Pardon E, Valant C, Sexton PM, Christopoulos A, Felder CC, Gmeiner P, Steyaert J, Weis WI, Garcia KC, Wess J, Kobilka BK. Activation and allosteric modulation of a muscarinic acetylcholine receptor. (2013) Nature 504, 101-106. *Equal contributors
  • Kruse AC, Li J, Hu J, Kobilka BK, Wess J. Novel insights into M3 muscarinic acetylcholine receptor physiology and structure. (2013) J. Mol. Neurosci. 53, 316 - 323.
  • Kruse AC, Manglik A, Kobilka BK, Weis WI. Applications of molecular replacement to G protein-coupled receptors. (2013) Acta Cryst. D69, 2287-2292.
  • Kruse AC*, Weiss DR*, Rossi M, Hu J, Hu K, Eitel K, Gmeiner P, Wess J, Kobilka BK, Shoichet BK. Muscarinic receptors as model targets and antitargets for structure-based ligand discovery. (2013) Mol. Pharm. 84, 528-540. *Equal contributors
  • Ring AM*, Manglik A*, Kruse AC*, Enos MD, Weis WI, Garcia KC, Kobilka BK. Adrenaline-activated structure of the β2-adrenoceptor stabilized by an engineered nanobody. (2013) Nature 502, 575-579. *Equal contributors
  • Chae PS, Kruse AC, Gotfryd K, Rana RR, Cho KH, Rasmussen SG, Bae HE, Chandra R, Gether U, Guan L, Kobilka BK, Loland CJ, Byrne B, Gellman SH. Novel Tripod Amphiphiles for Membrane Protein Analysis. (2013) Chem. Eur. J. 19, 15645-15651.
  • Shukla AK*, Manglik A*, Kruse AC*, Xiao K, Reis RI, Tseng WC, Staus DP, Hilger D, Uysal S, Huang LY, Paduch M, Tripathi-Shukla P, Koide A, Koide S, Weis WI, Kossiakoff AA, Kobilka BK, Lefkowitz RJ. Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide. (2013) Nature 497, 137-141. *Equal contributors
  • Chae PS, Rana RR, Gotfryd K, Rasmussen SG, Kruse AC, Cho KH, Capaldi S, Carlsson E, Kobilka BK, Loland CJ, Gether U, Banerjee S, Byrne B, Lee JK, Gellman SH. Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study. (2013) Chem. Commun. 49, 2287-2289.


  • Kruse AC, Hu J, Pan AC, Arlow DH, Rosenbaum DM, Rosemond E, Green HF, Liu T, Chae PS, Dror RO, Shaw DE, Weis WI, Wess J, Kobilka BK. Structure and dynamics of the M3 muscarinic acetylcholine receptor. (2012) Nature 482, 552-556.
  • Haga K*, Kruse AC*, Asada H*, Yurugi-Kobayashi T, Shiroishi M, Zhang C, Weis WI, Okada T, Kobilka BK, Haga T, Kobayashi T. Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist. (2012) Nature 482, 547-551. *Equal contributors
  • Granier S, Manglik A*, Kruse AC*, Kobilka TS, Thian FS, Weis WI, Kobilka BK. Crystal structure of the δ-opioid receptor bound to naltrindole. (2012) Nature 485, 400-404. *Equal contributors
  • Manglik A, Kruse AC, Kobilka TS, Thian FS, Mathiesen JM, Sunahara RK, Pardo L, Weis WI, Kobilka BK, Granier S. Crystal structure of the µ-opioid receptor bound to a morphinan antagonist. (2012) Nature 485, 321-326.
  • Chae PS, Rasmussen SG, Rana RR, Gotfryd K, Kruse AC, Manglik A, Cho KH, Nurva S, Gether U, Guan L, Loland CJ, Byrne B, Kobilka BK, Gellman SH. A new class of amphiphiles bearing rigid hydrophobic groups for solubilization and stabilization of membrane proteins. (2012) Chem. Eur. J. 18, 9485-9490.


  • Adams JJ, Narayanan S, Liu B, Birnbaum ME, Kruse AC, Bowerman NA, Chen W, Levin AM, Connolly JM, Zhu C, Kranz DM, Garcia KC. T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex. (2011) Immunity 35, 681-693.
  • Rasmussen SG, DeVree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, Thian FS, Chae PS, Pardon E, Calinski D, Mathiesen JM, Shah ST, Lyons JA, Caffrey M, Gellman SH, Steyaert J, Skiniotis G, Weis WI, Sunahara RK, Kobilka BK. Crystal structure of the β2 adrenergic receptor-Gs protein complex. (2011) Nature 477, 549-555.
  • Newell EW, Ely LK, Kruse AC, Reay PA, Rodriguez SN, Lin A, Kuhns MS, Garcia KC, Davis MM. Structural insight into the Specificity and Cross Reactivity of T Cell Receptors specific for Cytochrome c-I-Ek. (2011) J. Immunol. 186, 5823-5832.
  • Kruse AC, Huseby M, Shi K, Digre J, Ohlendorf DH, Earhart CA. Structure of a mutant beta toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility. (2011) Acta Cryst. F67, 438-441.


  • Chae PS, Rasmussen SGF, Rana R, Gotfryd K, Chandra R, Goren MA, Kruse AC, Nurva S, Loland CJ, Pierre Y, Drew D, Popot JL, Picot D, Fox BG, Guan L, Gether U, Byrne B, Kobilka B, Gellman SH. Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins. (2010) Nat. Methods 7, 1003-1008.
  • Chu HH, Moon JJ, Kruse AC, Pepper M, Jenkins MK. Negative Selection and Peptide Chemistry Determine the Size of Naive Foreign Peptide-MHC Class II-Specific CD4+ T Cell Populations. (2010) J. Immunol. 185, 4705-4713.
  • Huseby M, Kruse AC, Digre J, Mann EE, Bayles KW, Bohach GA, Schlievert PM, Ohlendorf DH, Earhart CA. Beta-toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms. (2010) Proc. Natl. Acad. Sci. U. S. A. 107, 14407-14412.
  • Hellberg K, Grimsrud PA, Kruse AC, Banaszak LJ, Ohlendorf DH, Bernlohr DA. X-ray crystallographic analysis of adipocyte fatty acid binding protein (aP2) modified with 4-hydroxy-2-nonenal. (2010) Protein Sci. 19, 1480-1489.


  • Hertzel AV, Hellberg K, Reynolds JM, Kruse AC, Juhlmann BE, Smith AJ, Sanders MA, Ohlendorf DH, Suttles J, Bernlohr DA. Identification and Characterization of a Small Molecule Inhibitor of Fatty Acid Binding Proteins. (2009) J. Med. Chem. 52, 6024-6031.


  • Yoder AR, Kruse AC, Earhart CA, Ohlendorf DH, Potter LR. Reduced ability of C-type natriuretic peptide (CNP) to activate natriuretic peptide receptor B (NPR-B) causes dwarfism in lbab -/- mice. (2008) Peptides. 29, 1575-1581.