3.4.11.9 8 mg/ml purified recombinant enzyme in Tris, pH 8.5, hanging drop vapour diffusion method, 0.003 ml mixed with 0.002 ml reservoir solution containing 25% PEG 4000, 0.1 M Tris-HCl, pH 8.0, 0.2 M sodium acetate, and 1 mM MnCl2, 1 month at 4°C, cryoprotectant is 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling 649232 3.4.11.9 hanging drop vapour diffusion method, using 20% (v/v) polyethylene glycol 400, 0.15 M CaCl2, and 100 mM HEPES (pH 7.5) 698788 3.4.11.9 in complex with inhibitor apstatin 667056 3.4.11.9 Mn(II)-form of enzyme and substituted with Mg2+, Zn2+, Ca2+, Na+ and apo-enzyme in complex with L-Val-L-Pro-L-Leu 667633 3.4.11.9 mutants E383A, H361A and H243A in complex with substrate L-Val-L-Pro-L-Leu. Substrate interacts with one of the active site metal ions via its terminal amino group 683096 3.4.11.9 mutants H243A, D260A, D271A, H350A, H354A, H361A, E383A 667743 3.4.11.9 oil microbatch method 753576 3.4.11.9 purified recombinant enzyme PfAPP both unliganded and in complex with inhibitor apstatin, hanging drop vapor diffusion method, mixing of 2:1 vl/v ratio of 6 mg/ml protein solution with reservoir containing 40-50% 2-methyl-2,4-pentanediol, and 0.1 M sodium cacodylate, pH 5.6-6.2, 3-7 days, X-ray diffraction structure determination and analysis at 2.30-2.35 A resolution. Crystals of the apstatin:PfAPP complex are obtained by soaking unliganded crystals in mother liquor supplemented with 2 mM apstatin for 1 h. For the unliganded PfAPP structure, the molecular replacement search model is prepared from the structure of human APP1 (PDB ID 3CTZ) 752716 3.4.11.9 purified recombinant enzyme, mixing of 0.002 ml of about 15 mg/ml protein in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, with 0.002 ml crystallization solution containing 0.1 M phospho-citrate, pH 4.6, 0.2 M NaCl, and 22% PEG 8000, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using the putative prolidase from Telmatobius sibiricus (PDB ID: 4FKC) as template 755354 3.4.11.9 purified recombinant enzyme, mixing of 0.002 ml of about 15 mg/ml protein in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, with 0.002 ml of crystallization solution containing 1.4 M trisodium citrate, 0.1 M sodium cacodylate, pH 6.5, 10% glycerol, and 0.5 mM ZnCl2, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using the putative prolidase from Telmatobius sibiricus (PDB ID: 4FKC) as template 755354 3.4.11.9 purified recombinant enzyme, X-ray diffraction structure determination and analysis at 1.78-1.85 A resolution 753683 3.4.11.9 purified recombinant His-tagged enzyme by sitting drop vapour diffusion method, crystallization buffer containing 17.5% PEG 3350, 0.1 M bis-tris propane, pH 8.5, and 0.2 M sodium malonate is mixed with an equal volume of 3 mg/ml protein in 10 mM Tris/HCl, pH 8.0, and 150 mM NaCl,16°C, X-ray diffraction structure determination and analysis at 1.93 A resolution 753579 3.4.11.9 purified recombinant His6-tagged enzyme, microbatch crystallization method, mixing of 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of crstallization solution containing 30% v/v PEG400, 0.1 M sodium acetate, 0.2 M calcium acetate, pH 4.5, the pH is adjusted to pH 5.8 with acetic acid, X-ray diffraction structure determination and analysis at 3.4 A, molecular replacement based on the structure of human prolidase (PDB ID 2IW2) 754700 3.4.11.9 XPD43 is crystallized to 1.83 A resolution using the microbatch-under-oil technique 731082