Edward Arnold And

نویسنده

MICHAEL G. ROSSMANN

چکیده

The structure of human rhinovirus 14 has been refined, by the method of restrained least squares, to an R factor of 0.16 for various random samples between 6 and 3 A, resolution with F > 3o-(F). As a first step the non-crystal lographic symmetry parameters were optimized using the initial atomic model * Present address: Center for Advanced Biotechnology and Medicine (CABM) and Department of Chemistry, Rutgers University, Piscataway, New Jersey 08855-0759, USA. 0108-7673/88/030270-13 $03.00 in a rigid-body refinement procedure. Phase determination by the molecular-replacement phase extension and refinement procedure was continued to 2.94 A, resolution, employing the improved non-crystallographic symmetry operators. The resultant structurefactor phases and weights, together with the measured ampli tudes, constituted the X-ray observations used in the restrained refinement. The Hendr icksonKonnert p rogram system [Konner t & Hendr ickson (1980). Acta Cryst. A36, 344-350] was modified to incorporate non-crystal lographic symmetry constraints and structure-factor phases as observations. O 1988 International Union of Crystallography EDWARD ARNOLD AND MICHAEL G. ROSSMANN 271 The non-bonded contacts between subunits related by non-crystallographic symmetry were also restrained.

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