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EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.1010 mg/ml purified enzyme, complexed with inhibitor L-leucinephosphonic acid from a 4fold molar excess, with precipitation solution containing Tris, pH 8.0, 10 mM KSCN, 0.4 M NaCl, 4 days, X-ray diffraction structure determination and analysis at 2.1 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.1016 mg/ml enzyme complexed with inhibitory Tris, in 10 mM Tris, pH 8.0, 10 mM KSCN, 0.4 NaCl, vapour diffusion method, with precipitant solution containing 100 mM Tris, pH 8.0, 100 mM KSCN, 4.5 M NaCl, 48 h, X-ray diffraction structure determination and analysis at 1.2 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.10analysis of crystal structures of free Zn-enzyme, and Zn-enyme bound to different inhibitors, complex optimizations, overview
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.10crystallization at pH 8.0 of enzyme in high salt Tris buffer against low salt concentration, X-ray diffraction crystal structure determination and analysis at 2.5 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.10free Zn-enzyme or enzyme in complex with synthetic inhibitor 4-iodo-D-phenylalanine hydroxamate, X-ray diffraction structure determination and analysis at 1.8 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.10hanging drop vapour diffusion method, aminopeptidase in 10 mM Tris buffer, pH 8.0, containing 10 mM KSCN and 400 mM NaCl is equilibrated with 100 mM Tris buffer, pH 8.0, containing 100 mM KSCN and 4.5 M NaCl, at 19°C
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.10hanging drop vapour diffusion method, at 25°C
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.10LAP in complex with bestatin is crystallized to 2.8 A resolution using the hanging-drop vapour-diffusion method
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.10purified enzyme free and in complex with inhibitor bestatin, enzyme bound with Zn2+ and Na+, hanging drop vapour-diffusion method, mixing of 0.002 ml of 11.2 mg/ml protein solution with 0.002 ml of reservoir solution containing 11% w/v PEG 3350 and 100 mM sodium formate, pH 7.0, and equilibration against reservoir solution, crystals of HpM17AP-bestatin complex are obtained by using 5.6 mg/ml protein, 1 mM bestatin and the reservoir solution containing 12% w/v PEG 2000 and 100 mM sodium formate, pH 7.0, 19°C, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution, molecular replacement using the structure of LAP from Pseudomonas putida (PDB ID 3h8g) as a search model
Display the word mapDisplay the reaction diagram Show all sequences 3.4.11.10purified enzyme in complex Tris, 16 mg/ml in 10 mM Tris, pH 8.0, 10 mM KSCN, and 0.4 M NaCl, hanging drop vapour diffusion method, precipitation solution contains 100 mM Tris, pH 8.0, 100 mM KSCN, and 4.5 M NaCl, 48 h, X-ray diffraction structure determination and analysis at 1.2 A resolution, modeling
Results 1 - 10 of 18 > >>