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86 citations found for Cascarano, G.L.
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The program SIR97 is a versatile tool for direct solution and complete refinement of crystal structures.

EXPO is a program for full powder pattern decomposition, crystal structure solution and phase refinement.

The efficiencies of Patterson and direct-methods techniques for substructure applications are compared.

A procedure is described for locating the anomalous scatterers in SAD and MAD cases.


Crystallographic least-squares techniques, a fundamental tool for crystal structure refinement, are used for the first time for ab initio crystal structure solution. No help was needed from other phasing techniques, such as the calculation of electron-density maps.

The probabilistic estimate of the amplitudes for normal scattering from the anomalous scattering substructure is attempted in the two-wavelength case.

Several early figures of merit (FOMs) are tested for their ability to speed up ab initio protein phasing. A new combined FOM is proposed.

The main features of the program SIR2011 are described.

A new triplet invariant formula is used to phase ab initio proteins with data at non-atomic resolution.

A new phasing approach able to solve ab initio protein structures via diffraction data at 1.4 Å resolution is described and tested.

A Patterson deconvolution procedure is applied to powder diffraction data. Its efficiency is compared with the performance of direct methods.

The phasing procedure of SIR2000 has been modified to improve efficiency and offer a wider applicability range.


An algorithm for predicting the most informative wavelength combination in the MAD case is described.

The VLD (vive la difference) phasing algorithm is combined with hybrid Fourier syntheses to solve ab initio small and medium-size structures and proteins.

A phase refinement procedure for ab initio structure solution with heavy atoms is described.

An overview of the main features and potentialities of the package SIR2004 is presented.

An improved algorithm for Patterson deconvolution has been tested and compared with direct-methods approaches for ab initio crystal structure solution of macromolecules.

New algorithms for solving ab initio protein crystal structures with data up to 1.4 Å are described and checked by experimental data.