Abstract
AbstractThe 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. Int J Quantum Chem, 2005
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