EC Number   |
|---|
    5.3.1.6 | 2.1 A resolution crystal structure. Crystals are cryo-protected by transfering through crystallization solution with progressively higher ethylene glycol concentration up to 30% v/v and then flash cooled in liquid nitrogen. The protein crystallizes in space group F432 with cell dimensions a = b = c = 209A, corresponding to one molecule per asymmetric unit and a solvent content of 47% |
| 5.3.1.6 | co-crystallization in the presence of 20 mM ribose-5-phosphate or 20 mM ribose-5-phosphate with 12 mM MnCl2, sitting drop vapor diffusion method, using 0.1 M Na citrate pH 5.0, 20% (w/v) PEG 6000 |
| 5.3.1.6 | comparison of structures and active sites of RpiB and RpiA from Homo sapiens (HsRpiA). Both enzymes form a homomultimer, which in the enzymes of type B is essential to form the active site. Distinct residue types participate in the catalytic reaction in the two enzymes. In LmRpiB, residues Y46,H11, H102 and H138 are part of the active site |
| 5.3.1.6 | comparison of structures and active sites of RpiB from Leishmania major and RpiA and docking of substrate. Both enzymes form a homomultimer, which in the enzymes of type B is essential to form the active site. Distinct residue types participate in the catalytic reaction in the two enzymes |
| 5.3.1.6 | crystal structure of enzyme complexed with the open chain form of the ribose 5-phosphate and the open chain form of the C2 epimeric inhibitor arabinose 5-phosphate as well as the apo form at high resolution |
| 5.3.1.6 | hanging drop vapor diffusion method, crystal structure of the free enzyme and the complex with D-4-phosphoerythronic acid |
| 5.3.1.6 | hanging drop vapor diffusion method, enzyme form RpiA |
| 5.3.1.6 | hanging drop vapor diffusion method, structure of a complex with arabinose 5-phosphate at 1.25 A resolution |
| 5.3.1.6 | hanging drop vapour diffusion method, X-ray structure of ribose-5-phosphate isomerase B in complex with the inhibitors 4-phosphono-D-erythronohydroxamate and 4-phospho-D-erythronate refined to resolutions of 2.1 and 2.2 A |
| 5.3.1.6 | homology modeling of wild type and mutants |
