C. Marck and H. Grosjean, tRNomics: Analysis of tRNA genes from 50 genomes of Eukarya, Archaea, and Bacteria reveals anticodon-sparing strategies and domain-specific features, RNA, vol.8, issue.10, pp.1189-1232, 2002.
DOI : 10.1017/S1355838202022021

P. Wrede, N. H. Woo, and A. Rich, Initiator tRNAs have a unique anticodon loop conformation., Proc. Natl Acad. Sci. USA, pp.3289-3293, 1979.
DOI : 10.1073/pnas.76.7.3289
URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC383810/pdf

B. L. Seong and U. L. Rajbhandary, Escherichia coli formylmethionine tRNA: mutations in GGGCCC sequence conserved in anticodon stem of initiator tRNAs affect initiation of protein synthesis and conformation of anticodon loop., Proc. Natl Acad. Sci. USA, pp.334-338, 1987.
DOI : 10.1073/pnas.84.2.334

D. Hartz, J. Binkley, T. Hollingsworth, and L. Gold, Domains of initiator tRNA and initiation codon crucial for initiator tRNA selection by Escherichia coli IF3., Genes & Development, vol.4, issue.10, pp.1790-1800, 1990.
DOI : 10.1101/gad.4.10.1790

U. Varshney, C. P. Lee, and U. L. Rajbhandary, From elongator tRNA to initiator tRNA., Proc. Natl Acad. Sci. USA, pp.2305-2309, 1993.
DOI : 10.1073/pnas.90.6.2305

R. Basavappa and P. B. Sigler, The 3 A crystal structure of yeast initiator tRNA: functional implications in initiator/elongator discrimination, EMBO J, vol.10, pp.3105-3111, 1991.

N. H. Woo, B. A. Roe, and A. Rich, Three-dimensional structure of Escherichia coli initiator tRNAfMet, Nature, vol.6, issue.5771, pp.346-351, 1980.
DOI : 10.1038/286346a0

D. C. Schweisguth and P. B. Moore, On the conformation of the anticodon loops of initiator and elongator methionine tRNAs, Journal of Molecular Biology, vol.267, issue.3, pp.505-519, 1997.
DOI : 10.1006/jmbi.1996.0903

M. Selmer, C. M. Dunham, F. V. Murphy, A. Weixlbaumer, S. Petry et al., Structure of the 70S Ribosome Complexed with mRNA and tRNA, Science, vol.313, issue.5795, pp.1935-1942, 2006.
DOI : 10.1126/science.1131127

A. Korostelev, S. Trakhanov, M. Laurberg, and H. F. Noller, Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements, Cell, vol.126, issue.6, pp.1065-1077, 2006.
DOI : 10.1016/j.cell.2006.08.032

M. M. Yusupov, G. Z. Yusupova, A. Baucom, K. Lieberman, T. N. Earnest et al., Crystal Structure of the Ribosome at 5.5 A Resolution, Science, vol.292, issue.5518, pp.883-896, 2001.
DOI : 10.1126/science.1060089

A. Korostelev and H. F. Noller, The ribosome in focus: new structures bring new insights, Trends in Biochemical Sciences, vol.32, issue.9, pp.434-441, 2007.
DOI : 10.1016/j.tibs.2007.08.002

P. Nissen, J. A. Ippolito, N. Ban, P. B. Moore, and T. A. Steitz, RNA tertiary interactions in the large ribosomal subunit: The A-minor motif, Proc. Natl Acad. Sci. USA, pp.4899-4903, 2001.
DOI : 10.1073/pnas.081082398

N. M. Abdi and K. Fredrick, Contribution of 16S rRNA nucleotides forming the 30S subunit A and P sites to translation in Escherichia coli, RNA, vol.11, issue.11, pp.1624-1632, 2005.
DOI : 10.1261/rna.2118105

L. Lancaster and H. F. Noller, Involvement of 16S rRNA Nucleotides G1338 and A1339 in Discrimination of Initiator tRNA, Molecular Cell, vol.20, issue.4, pp.623-632, 2005.
DOI : 10.1016/j.molcel.2005.10.006

D. Mangroo, P. A. Limbach, J. A. Mccloskey, and U. L. Rajbhandary, An anticodon sequence mutant of Escherichia coli initiator tRNA: possible importance of a newly acquired base modification next to the anticodon on its activity in initiation., Journal of Bacteriology, vol.177, issue.10, pp.2858-2862, 1995.
DOI : 10.1128/jb.177.10.2858-2862.1995

A. G. Leslie, The integration of macromolecular diffraction data, Acta Crystallographica Section D Biological Crystallography, vol.62, issue.1, pp.48-57, 2006.
DOI : 10.1107/S0907444905039107

P. Evans, Scaling and assessment of data quality, Acta Crystallographica Section D Biological Crystallography, vol.62, issue.1, pp.72-82, 2006.
DOI : 10.1107/S0907444905036693

A. J. Mccoy, R. W. Grosse-kunstleve, L. C. Storoni, and R. J. Read, Likelihood-enhanced fast translation functions, Acta Crystallographica Section D Biological Crystallography, vol.61, issue.4, pp.458-464, 2005.
DOI : 10.1107/S0907444905001617

P. Emsley and K. Cowtan, : model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.2126-2132, 2004.
DOI : 10.1107/S0907444904019158

M. D. Winn, M. N. Isupov, and G. N. Murshudov, Use of TLS parameters to model anisotropic displacements in macromolecular refinement, Acta Crystallographica Section D Biological Crystallography, vol.57, issue.1, pp.122-133, 2001.
DOI : 10.1107/S0907444900014736

G. N. Murshudov, A. A. Vagin, and E. J. Dodson, Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.3, pp.240-255, 1997.
DOI : 10.1107/S0907444996012255

M. Strong, M. R. Sawaya, S. Wang, M. Phillips, D. Cascio et al., Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis, Proc. Natl Acad. Sci. USA, pp.8060-8065, 2006.
DOI : 10.1073/pnas.0602606103

S. H. Kim, G. J. Quigley, F. L. Suddath, A. Mcpherson, D. Sneden et al., Three-Dimensional Structure of Yeast Phenylalanine Transfer RNA: Folding of the Polynucleotide Chain, Science, vol.179, issue.4070, pp.285-288, 1973.
DOI : 10.1126/science.179.4070.285

D. Moras, A. C. Dock, P. Dumas, E. Westhof, P. Romby et al., Anticodon-anticodon interaction induces conformational changes in tRNA: yeast tRNAAsp, a model for tRNA-mRNA recognition., Proc. Natl Acad. Sci. USA, pp.932-936, 1986.
DOI : 10.1073/pnas.83.4.932

P. Auffinger and E. Westhof, Singly and Bifurcated Hydrogen-bonded Base-pairs in tRNA Anticodon Hairpins and Ribozymes, Journal of Molecular Biology, vol.292, issue.3, pp.467-483, 1999.
DOI : 10.1006/jmbi.1999.3080

E. Schmitt, M. Panvert, S. Blanquet, and Y. Mechulam, Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet, The EMBO Journal, vol.286, issue.23, pp.6819-6826, 1998.
DOI : 10.1093/emboj/17.23.6819

P. C. Durant and D. R. Davis, Stabilization of the anticodon stem-loop of tRNALys,3 by an A+-C base-pair and by pseudouridine, Journal of Molecular Biology, vol.285, issue.1, pp.115-131, 1999.
DOI : 10.1006/jmbi.1998.2297

H. Wakao, P. Romby, E. Westhof, S. Laalami, M. Grunberg-manago et al., The solution structure of the Escherichia coli initiator tRNA and its interactions with initiation factor 2 and the ribosomal 30 S subunit, J. Biol. Chem, vol.264, pp.20363-20371, 1989.

J. D. Robertus, J. E. Ladner, J. T. Finch, D. Rhodes, R. S. Brown et al., Structure of yeast phenylalanine tRNA at 3 ??? resolution, Nature, vol.1, issue.5467, pp.546-551, 1974.
DOI : 10.1038/250546a0

F. L. Suddath, G. J. Quigley, A. Mcpherson, D. Sneden, J. J. Kim et al., Three-dimensional structure of yeast phenylalanine transfer RNA at 3. 0??? resolution, Nature, vol.97, issue.5443, pp.20-24, 1974.
DOI : 10.1038/248020a0

L. Jovine, S. Djordjevic, and D. Rhodes, The crystal structure of yeast phenylalanine tRNA at 2.0 ?? resolution: cleavage by Mg2+ in 15-year old crystals, Journal of Molecular Biology, vol.301, issue.2, pp.401-414, 2000.
DOI : 10.1006/jmbi.2000.3950

H. Shi and P. B. Moore, The crystal structure of yeast phenylalanine tRNA at 1.93 ??? resolution: A classic structure revisited, RNA, vol.6, issue.8, pp.1091-1105, 2000.
DOI : 10.1017/S1355838200000364

E. Westhof, P. Dumas, and D. Moras, Crystallographic refinement of yeast aspartic acid transfer RNA, Journal of Molecular Biology, vol.184, issue.1, pp.119-145, 1985.
DOI : 10.1016/0022-2836(85)90048-8

P. Benas, G. Bec, G. Keith, R. Marquet, C. Ehresmann et al., The crystal structure of HIV reverse-transcription primer tRNA(Lys,3) shows a canonical anticodon loop, RNA, vol.6, issue.10, pp.1347-1355, 2000.
DOI : 10.1017/S1355838200000911

V. Ramesh, C. Mayer, M. R. Dyson, S. Gite, and U. L. Rajbhandary, Induced fit of a peptide loop of methionyl-tRNA formyltransferase triggered by the initiator tRNA substrate, Proc. Natl Acad. Sci. USA, pp.875-880, 1999.
DOI : 10.1073/pnas.96.3.875

V. Berk, W. Zhang, R. D. Pai, and J. H. Cate, Structural basis for mRNA and tRNA positioning on the ribosome, Proc. Natl Acad. Sci. USA, pp.15830-15834, 2006.
DOI : 10.1073/pnas.0607541103

A. Dallas and H. F. Noller, Interaction of Translation Initiation Factor 3 with the 30S Ribosomal Subunit, Molecular Cell, vol.8, issue.4, pp.855-864, 2001.
DOI : 10.1016/S1097-2765(01)00356-2