A simulation of a protein powder diffraction pattern was stunning in the apparent amount of information that was seen. A subsequent experiment on metmyoglobin gave a powder diffraction pattern that showed very little sample broadening; the peak widths were essentially limited by the instrument resolution. The challenge is to make use of this in protein structure analysis. This talk will recall some of those early experiments and data analyses as well as an overview of current progress and future possibilities.

Supported by US DOE/OS/BES under Contract No. DE-AC-02-06CH11357.

• Legal notice:
  

  Copyright (c) Pielaszek Research, all rights reserved.
  The above materials, including auxiliary resources, are subject to Publisher's copyright and the Author(s) intellectual rights. Without limiting Author(s) rights under respective Copyright Transfer Agreement, no part of the above documents may be reproduced without the express written permission of Pielaszek Research, the Publisher. Express permission from the Author(s) is required to use the above materials for academic purposes, such as lectures or scientific presentations.
  In every case, proper references including Author(s) name(s) and URL of this webpage: https://science24.com/paper/15453 must be provided.

1. Macromolecular powder diffraction: Structure solution via molecular replacement