Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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BIOLOGICAL
CRYSTALLOGRAPHY

Volume 49| Part 1

ISSN: 1399-0047

January 1993 issue

Cover illustration: Stereoview of a fragment of DNA form B. Courtesy of A. Soyer.

international union of crystallography

Biological crystallography

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Preface

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research papers

Phasing macromolecular structures via structure-invariant algebra

H. Hauptman and F. Han

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On the application of phase relationships to complex structures. XXXII. A small protein at low resolution

M. Mukherjee and M. M. Woolfson

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On the application of phase relationships to complex structures. XXXIII. The problems with large structures and low resolution

M. M. Woolfson

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The application of direct methods and Patterson interpretation to high-resolution native protein data

G. M. Sheldrick, Z. Dauter, K. S. Wilson, H. Hope and L. C. Sieker

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Assessment of phase accuracy by cross validation: the free R value. Methods and applications

A. T. Brünger

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Direct phase determination by entropy maximization and likelihood ranking: status report and perspectives

G. Bricogne

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Construction of maximum-entropy density maps, and their use in phase determination and extension

E. Prince

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Experience with phase extension and ab initio phase determination in macromolecular crystallography using maximum-entropy methods

L. Sjölin and L. A. Svensson

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Entropy phase dynamics

A. D. McLachlan

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Entropy on charge density: making the quantum mechanical connection

D. M. Collins

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Electron-denisty histograms and the phase problem

V. Yu. Lunin

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Programs for phasing by entropy maximization as implemented in Xtal3.2: a crystallographic software system

J. M. Stewart, D. M. Collins, K. D. Watenpaugh, E. Prince and S. R. Hall

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Discussion after talk by J. M. Stewart

D. Sayre

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Low-resolution real-space envelopes: improvements to the condensing protocol approach and a new method to fix the sign of such envelopes

S. Subbiah

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Towards the measurement of ideal data for macromolecular crystallography using synchrotron sources

J. R. Helliwell, S. Ealick, P. Doing, T. Irving and M. Szebenyi

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Automated refinement of protein models

V. S. Lamzin and K. S. Wilson

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Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints

K. D. Cowtan and P. Main

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Ab initio direct methods: practical advice for getting beyond the first 300 atoms

D. A. Langs

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Molecular scene analysis: the integration of direct-methods and artificial-intelligence strategies for solving protein crystal structure

S. Fortier, I. Castleden, J. Glasgow, D. Conklin, C. Walmsley, L. Leherte and F. H. Allen

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Application of the minimal principle to peptide structures

C. M. Weeks, G. T. DeTitta, R. Miller and H. A. Hauptman

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The effect of noise on entropy

R. Swanson and S. M. Swanson

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Uniqueness and the ab initio phase problem in macromolecular crystallography

D. Baker, A. E. Krukowski and D. A. Agard

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Entropy maximization constrained by solvent flatness: a new method for macromolecular phase extension and map improvement

S. Xiang, C. W. Carter Jnr, G. Bricogne and C. J. Gilmore

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SQUASH – combining constraints for macromolecular phase refinement and extension

K. Y. J. Zhang

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