Crystals of the BCL-xL-p53-DBD fusion protein were grown at 18 °C by the hanging-drop method with a reservoir buffer of 0.2 M sodium malonate pH 7.0 and 20% polyethylene glycol 3,350 (w/v) (Hampton Research, HR2-126). For data collection, a single crystal was soaked in well solution plus 20% glycerol (v/v) and flash-frozen in liquid nitrogen. Data were collected at the BL17U43 and BL19U144 beamlines of Shanghai Synchrotron Radiation Facility (SSRF). Then the data were processed using HKL200045. The structure was solved by molecular replacement with phaser from PHENIX package46 using the previously solved p53 structure (PDB: 3KMD)4 and BCL-xL structure (PDB: 2YXJ)22 as search templates. Then the structure was refined with phenix.refine and model building was performed using WinCoot47. Translational-liberation-screw (TLS) refinement was used during the last stages of refinement. Graphical representations of the structure were generated using PyMOL48. The statistics of the crystallographic analysis are presented in Supplementary Table 1.

Note: The content above has been extracted from a research article, so it may not display correctly.



Q&A
Please log in to submit your questions online.
Your question will be posted on the Bio-101 website. We will send your questions to the authors of this protocol and Bio-protocol community members who are experienced with this method. you will be informed using the email address associated with your Bio-protocol account.



We use cookies on this site to enhance your user experience. By using our website, you are agreeing to allow the storage of cookies on your computer.