EC Number   |
|---|
  2.7.7.70 | purified SeMet-labeled and wild-type His6-tagged enzymes are crystallized from 0.1 M HEPES, pH 7.0, 20% w/v PEG 3350, 8.5 mM n-octyl-beta-D-thiomaltoside, and from 0.1 M MES, pH 6.5, 15% w/v PEG 3350, and 6-cyclohexyl-L-hexyl-beta-D-maltoside, respectively, hanging drop vapour diffusion method, X-ray diffraction structure determination and analysis at 2.80 A and 2.40 A resolution, respectively, modeling, the refined model of SeMet-BpHldC is used as a search model for molecular replacement (MR) to solve the structure of native BpHldC |
| 2.7.7.70 | purified SeMet-labeled enzyme containing a noncleavable N-terminal His6-tag, hanging drop vapour diffusion method, mixing of 800 nl of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 0.35 M NaCl with 800 nl of reservoir solution containing 0.1 M HEPES, pH 7.0, 20% w/v PEG 3350, and 8.5 mM n-octyl-beta-D-thiomaltoside, and equilibration over 0.05 ml of reservoir solution, room temperature, method optimization, X-ray diffraction structure determination and analysis at 2.80 A resolution, rod-shaped crystals, automated model building |
