title: Accurate charge density of the tripeptide Ala-Pro-Ala with the maximum entropy method (MEM): influence of data resolution.
abstract: The accurate electron density of Ala-Pro-Ala is determined by the maximum entropy method (MEM), employing the same reflection data measured at 100 K which was used for a multipole refinement by Kalinowski et al. [(2007), Acta Cryst. Accepted for publication]. Properties of the electron density are compared with the corresponding properties of the static electron density from the multipole model and to the dynamic MEM electron density of trialanine at 20 K. It is thus shown that the increased thermal smearing at 100 K leads to lower electron densities in the bond critical points and atomic charges closer to zero for Ala-Pro-Ala than has been obtained for trialanine at 20 K. The influence of the resolution of the data is investigated by a series of MEM calculations. Atomic charges and atomic volumes are found not to depend on the resolution, but the charge density in the BCPs decreases with decreasing resolution of the dataset. The origin of this dependence is found to lie mostly in the more accurate estimate of the atomic displacement parameters (ADPs) for the higher-resolution datasets. If these effects are taken into account, meaningful information on chemical bonding can be obtained with data at a resolution better than d(min) = 0.63 A. Alternatively, low-resolution X-ray diffraction data can be used in accurate electron-density studies by the MEM, if another source of accurate values of the ADPs is available, e.g. from refinements with multipole parameters from a database of transferable multipole parameters.
authors.affiliation: Laboratory of Crystallography, University of Bayreuth, Universitatstrasse 30, D-95440 Bayreuth, Germany.
authors.forename: Andreas
authors.initials: A
authors.lastname: Hofmann
authors.forename: Roman
authors.initials: R
authors.lastname: Kalinowski
authors.forename: Peter
authors.initials: P
authors.lastname: Luger
authors.forename: Sander
authors.initials: S
authors.lastname: van Smaalen
mesh_terms: D000409:Alanine / Q000737:chemistry*; D018360:Crystallography, X-Ray / Q000379:methods*; D003627:Data Interpretation, Statistical; D004583:Electrons; D019277:Entropy; D006860:Hydrogen Bonding; D015233:Models, Statistical; D008968:Molecular Conformation; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry*; D011487:Protein Conformation; D012984:Software; D013696:Temperature; D014961:X-Ray Diffraction
chemical_list: D010455:Peptides; D011392:Proline; D000409:Alanine