EC Number   |
|---|
   3.4.11.1 | - |
| 3.4.11.1 | crystal structure of XoLAP is determined at 2.6 A resolution. The XoLAP crystal contains two complete monomers in its asymmetric unit |
| 3.4.11.1 | crystallization in presence of ZnSO4, NaCl, and 2-methyl-2,4-pentanediol, at pH 7.8 in Tris buffer, X-ray diffraction crystal structure determination and analysis at 1.6 A resolution |
| 3.4.11.1 | hanging drop vapour diffusion method. The crystal structure of microginin FR1 from Microcystis sp. bound to bovine lens leucine aminopeptidase is established at 1.73 A resolution |
| 3.4.11.1 | purified recombinant His-tagged enzyme LmLAP-A, in the presence of Mn2+, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement, modelling |
| 3.4.11.1 | purified recombinant His-tagged enzyme LmLAP-A, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement, modelling. TcLAP-A crystallizes exclusively under citratecontaining conditions, which leads to the absence of one or both Mn2x02 ions from the active site and hence no electron density for the inhibitors |
| 3.4.11.1 | purified recombinant His-tagged enzyme TbLAP-A in complex with inhibitor bestatin, in the presence of ZnCl2 and Mn2+, X-ray diffraction structure determination and analysis, molecular replacement, modelling |
| 3.4.11.1 | sitting drop vapor diffusion method. The quaternary structure is built by dimers with a length of 100 A that form the edges of the tetrahedron. All 12 active sites are located on the inside of the tetrahedron. Substrate access is granted by pores with a maximal diameter of 10 A, allowing only small peptides and unfolded proteins access to the active site |
| 3.4.11.1 | the crystal structure of of the enzyme is determined at 1.6 A resolution in native form and in complex with the inhibitor amastatin, hanging drop, vapour-diffusion method |
| 3.4.11.1 | unliganded crystal structure of LAP-A is determined to 2.20 A resolution |
