M. Tambasco-studart, Vitamin B6 biosynthesis in higher plants, Proceedings of the National Academy of Sciences of the United States of America, vol.102, pp.13687-13692, 2005.

G. Guedez, Assembly of the Eukaryotic PLP-Synthase Complex from Plasmodium and Activation of the Pdx1 Enzyme, Structure, vol.20, pp.172-184, 2012.

A. M. Smith, W. C. Brown, E. Harms, and J. L. Smith, Crystal Structures Capture Three States in the Catalytic Cycle of a Pyridoxal Phosphate (PLP) Synthase, The Journal of biological chemistry, vol.290, pp.5226-5239, 2015.

F. Zein, Structure of the PLP Synthase Holoenzyme from Thermatoga Maritima, Biochemistry, vol.45, pp.14609-14620, 2006.

S. Wallner, M. Neuwirth, K. Flicker, I. Tews, and P. Macheroux, Dissection of Contributions from Invariant Amino Acids to Complex Formation and Catalysis in the Heteromeric Pyridoxal 5-Phosphate Synthase Complex from Bacillus subtilis, Biochemistry, vol.48, pp.1928-1935, 2009.

M. Gengenbacher, Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum: biochemical and structural insights, The Journal of biological chemistry, vol.281, pp.3633-3641, 2006.

F. M. Raushel, J. B. Thoden, and H. M. Holden, Enzymes with Molecular Tunnels, Accounts of Chemical Research, vol.36, pp.539-548, 2003.

J. W. Hanes, I. Keresztes, and T. P. Begley, Trapping of a chromophoric intermediate in the Pdx1-catalyzed biosynthesis of pyridoxal 5'-phosphate

, Angewandte Chemie, vol.47, pp.2102-2105, 2008.

X. Zhang, Structural Insights into the Catalytic Mechanism of the Yeast Pyridoxal 5-Phosphate Synthase Snz1, The Biochemical journal, vol.432, pp.445-450, 2010.

D. Von-stetten, In crystallo optical spectroscopy (icOS) as a complementary tool on the macromolecular crystallography beamlines of the ESRF, Acta crystallographica. Section D, Biological crystallography, vol.71, pp.15-26, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01131843

M. Ho, J. Menetret, H. Tsuruta, and K. N. Allen, The origin of the electrostatic perturbation in acetoacetate decarboxylase, Nature, vol.459, pp.393-397, 2009.

V. Borshchevskiy, Low-dose X-ray radiation induces structural alterations in proteins, Acta crystallographica. Section D, Biological crystallography, vol.70, pp.2675-2685, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01130625

A. P. Dubnovitsky, R. B. Ravelli, A. N. Popov, and A. C. Papageorgiou, Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage, Protein science : a publication of the Protein Society, vol.14, pp.1498-1507, 2005.

M. Weik, Specific Chemical and Structural Damage to Proteins Produced by Synchrotron Radiation Proceedings of the National Academy of, Sciences of the United States of America, vol.97, pp.623-628, 2000.

A. R. Pearson and R. L. Owen, Combining X-ray crystallography and SingleCrystal Spectroscopy to Probe Enzyme Mechanisms, Biochemical Society Transactions, vol.37, pp.378-381, 2009.

G. I. Berglund, The Catalytic Pathway of Horseradish Peroxidase at High Resolution, Nature, vol.417, pp.463-468, 2002.

O. B. Zeldin, M. Gerstel, and E. F. Garman, Optimizing the Spatial Distribution of Dose in X-Ray Macromolecular Crystallography, Journal of Synchrotron Radiation, vol.20, pp.49-57, 2013.

J. Foadi, Clustering Procedures for the Optimal Selection of Data Sets from Multiple Crystals in Macromolecular Crystallography, Acta Crystallographica Section D, vol.69, pp.1617-1632, 2013.

B. Derrer, Defining the structural requirements for ribose 5-phosphatebinding and intersubunit cross-talk of the malarial pyridoxal 5-phosphate synthase, FEBS Letters, vol.584, pp.4169-4174, 2010.

T. Raschle, Intersubunit Cross-Talk in Pyridoxal 5'-Phosphate Synthase, Coordinated by the C Terminus of the Synthase Subunit, The Journal of biological chemistry, vol.284, pp.7706-7718, 2009.

C. Moccand, M. Kaufmann, and T. B. Fitzpatrick, It takes two to tango: defining an essential second active site in pyridoxal 5'-phosphate synthase, PloS one, vol.6, p.16042, 2011.

N. Nagano, C. A. Orengo, and J. M. Thornton, One Fold with Many Functions: The Evolutionary Relationships between TIM Barrel Families Based on their Sequences, Structures and Functions, Journal of Molecular Biology, vol.321, pp.741-765, 2002.

S. B. Reeksting, Exploring inhibition of Pdx1, a component of the PLP synthase complex of the human malaria parasite Plasmodium falciparum, The Biochemical journal, vol.449, pp.175-187, 2013.

M. Neuwirth, X-Ray Crystal Strucuture of Saccharomyces cerevisiae Pdx1 Provides Insights into the Oligomeric Nature of PLP Synthases, FEBS Letters, vol.583, pp.2179-2186, 2009.

S. Jenni, Structure of fungal fatty acid synthase and implications for iterative substrate shuttling, Science, vol.316, pp.254-261, 2007.

N. Wu, S. Y. Tsuji, D. E. Cane, and C. Kholsa, Assessing the Balance between Protein-Protein Interactions and Enzyme-Substrate Interactions in the Channeling of Intermediates between Polyketide Synthase Modules, Journal of the American Chemical Society, vol.123, pp.6466-6475, 2001.

A. Tanovic, S. A. Samel, L. Essen, and M. A. Marahiel, Crystal Structure of the Termination Module of a Nonribosomal Peptide Synthetase, Science, vol.321, pp.659-663, 2008.

S. Pares, C. Cohen-addad, L. Sieker, M. Neuburger, and R. Douce, X-ray crystal structure determination at 2.6-A resolution of a lipoate-containing protein: The H-protein of the glycine decarboxylase complex from pea leaves, Proceedings of the National Academy of Sciences of the United States of America, vol.91, pp.4850-4853, 1994.

L. J. Reed and . Multienzyme-complexes, Accounts of Chemical Research, vol.7, pp.40-46, 1974.

J. Mcgeehan, Colouring cryo-cooled crystals: online microspectrophotometry, Journal of Synchrotron Radiation, vol.16, pp.163-172, 2009.

W. X. Kabsch, Acta crystallographica. Section D, Biological crystallography, vol.66, pp.125-132, 2010.

P. R. Evans and G. N. Murshudov, How good are my data and what is the resolution?, Acta crystallographica. Section D, Biological crystallography, vol.69, pp.1204-1214, 2013.

R. J. Gildea, New methods for indexing multi-lattice diffraction data, Acta crystallographica. Section D, Biological crystallography, vol.70, pp.2652-2666, 2014.

A. Vagin and A. Teplyakov, MOLREP: an Automated Program for Molecular Replacement, Journal of Applied Crystallography, vol.30, pp.1022-1025, 1997.

P. Emsley and K. Cowtan, Coot: Model-Building Tools for Molecular Graphics, Acta Crystallographica Section D, vol.60, pp.2126-2132, 2004.

G. N. Murshudov, A. A. Vagin, and E. J. Dodson, Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D, vol.53, pp.240-254, 1997.

P. D. Adams, The Phenix software for automated determination of macromolecular structures, Methods, vol.55, pp.94-106, 2011.

A. A. Lebedev, JLigand: a graphical tool for the CCP4 template-restraint library, Acta crystallographica. Section D, Biological crystallography, vol.68, pp.431-440, 2012.

M. D. Winn, Overview of the CCP4 suite and current developments, Acta crystallographica. Section D, Biological crystallography, vol.67, pp.235-242, 2011.

O. B. Zeldin, M. Gerstel, and E. F. Garman, RADDOSE-3D: time- and spaceresolved modelling of dose in macromolecular crystallography, Journal of Applied Crystallography, vol.46, pp.1225-1230, 2013.

A. T. Brunger, Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination, Acta Crystallographica Section D, vol.54, pp.905-921, 1998.

P. Emsley, B. Lohkamp, W. G. Scott, and K. Cowtan, Features and development of Coot, Acta crystallographica. Section D, Biological crystallography, vol.66, pp.486-501, 2010.

A. C. Wallace, R. A. Laskowski, and J. M. Thornton, LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions, Protein Engineering, vol.8, pp.127-134, 1995.

T. B. Fitzpatrick, Two independent routes of de novo vitamin B6 biosynthesis: not that different after all, The Biochemical journal, vol.407, pp.1-13, 2007.

G. Guedez, Assembly of the Eukaryotic PLP-Synthase Complex from Plasmodium and Activation of the Pdx1 Enzyme, Structure, vol.20, pp.172-184, 2012.

A. M. Smith, W. C. Brown, E. Harms, and J. L. Smith, Crystal Structures Capture Three States in the Catalytic Cycle of a Pyridoxal Phosphate (PLP) Synthase, The Journal of biological chemistry, vol.290, pp.5226-5239, 2015.

D. Von-stetten, In crystallo optical spectroscopy (icOS) as a complementary tool on the macromolecular crystallography beamlines of the ESRF, Acta crystallographica. Section D, Biological crystallography, vol.71, pp.15-26, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01131843

J. Foadi, Clustering Procedures for the Optimal Selection of Data Sets from Multiple Crystals in Macromolecular Crystallography, Acta Crystallographica Section D, vol.69, pp.1617-1632, 2013.

J. Mcgeehan, Colouring cryo-cooled crystals: online microspectrophotometry, Journal of Synchrotron Radiation, vol.16, pp.163-172, 2009.

A. T. Brunger, Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination, Acta Crystallographica Section D, vol.54, pp.905-921, 1998.

P. Emsley, B. Lohkamp, W. G. Scott, and K. Cowtan, Features and development of Coot, Acta crystallographica. Section D, Biological crystallography, vol.66, pp.486-501, 2010.

A. C. Wallace, R. A. Laskowski, and J. M. Thornton, LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions, Protein Engineering, vol.8, pp.127-134, 1995.