Hello everyone, Please forgive my ignorance about the field of crystallography. I have recently started to process the diffraction data of a protein with a ligand attached to it. we have the structure of this protein already known and also known with different ligands. the way I did it is as flllows:
I process the images in mosflm and then integrate them using scala inccp4i. After that I do molecular replacement by phaser. and finally refine it using refmac. Am I doing it correctly? Now since I am completely new to all this, I have not much clue about the outputs I get and if they are correct or not. What are the key things you should be looking at in the log files generated by phaser and refmac? Till now I get overall R factor of 29.32 and Rfree of 34.94. Is this fine or can I improve it more? If yes then what do I do to further improve the statistics? What should be the RmsBond and Rms Angle values? Since the structure is already solved a number of times with different ligands, what final values should i aim for to get a decent density maps in which I can fit my ligand structure. Sorry for being so naive. Any sort of information or papers or links would be very helpful. Thanks a lot. AA