Frontier example in experimental charge density research: Experimental electrostatics of proteins

Abstract

The experimental charge density methodology is extended to macromolecular structure and biocrystallography. Ultrahigh-resolution diffraction data now can be collected at third-generation synchrotron sources for well-ordered protein crystals; the data can be refined with a more sophisticated model than the independent atom model (IAM), such as the multipolar atom. A new crystallographic program MoPro combining small molecules and macromolecular refinement method has been developed; first applications are described. © 2004 Wiley Periodicals, Inc.