Dear Yang,
I have a protein which has the function unit as a dimer. I got two structures of it. One is the native structure, one is the mutant structure. Both structures are dimer in ASU. In the native structure the two chain look the same, but in mutant structure one chain still keep the same structure as the native one, and another chain is different. We expect to see the difference, but we wonder why one chain is different and another one is the same? Is this because of crystallographic packing?
Are both space groups between both structures the same? What about the cell dimensions? You might want to check the crystal contacts, the neighboring molecules in both structures. You might have some differences in the region where you can see some variations. Is it a point mutation, or is it a deleted mutant? What about the temperature factors of the all proteins and of the region where you found some differences? How did you solve the structure of the mutant? Molecular replacement using the coordinates of the native structure? Did you try to refine without the variable region to check if the conformation (which ever) is true? Please give more informations.
HTH anyway. Kind regards. Leo ------------------------------------------------------------ Chavas Leonard, Ph.D. Research Associate ------------------------------------------------------------ Faculty of Life Sciences The University of Manchester The Michael Smith Building Oxford Road Manchester Lancashire M13 9PT ------------------------------------------------------------ Tel: +44(0)161-275-1586 e-mail: [EMAIL PROTECTED]
