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Errors in data and complexity of structure are comparatively unimportant in the success of direct methods in solving oligonucleotides. The main factors for success are high-resolution data or, at lower resolutions, the presence of heavy atoms

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The P atoms in oligonucleotide crystals can be located by using anomalous-scattering differences, |δF|, in the direct-methods program MULTAN. Success is not dependent on having high- resolution data, but the errors in the |δF|'s must be small.

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In solution small-angle X-ray scattering data, the lowest-angle region is affected by interparticle correlations and potentially provides information concerning particle-particle interactions in solution, such as overall electrostatic interaction- attractive or repulsive - and tendency to form aggregates. A method is presented, based on a Monte Carlo approach, to calculate the interparticle interference for a solution of particles of arbitrary shape interacting through a simple two-particle hard-core potential. The method provides a basis for a quantitative analysis of the concentration-dependent scattering in the low-angle region. It has been used to study the relative effects of interparticle interference and particle dimerization in the scattering profiles for the proteins troponin C and lysozyme. The calculation may be generalized to include a more physically realistic potential.

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