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Physical measurement of triplet invariants: present state of the experiment, data evaluation and future perspectives
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E. Weckert
Published/Copyright:
September 25, 2009
Abstract
Invariant triplet phases can be determined experimentally by multi-beam interference experiments. In favourable conditions phases can also be determined from crystals of small macromolecules. The phase error is quite small, provided crystals of good quality are available. Single phases can be derived from triplet phases by means of maximum entropy based statistical methods. The number of experimental triplet phases necessary to solve a small protein crystal structure can be reduced by the application of an automatic refinement procedure. About 2.5 reflection phases per residue are necessary to solve the structure of a small protein if a high-resolution intensity data set is available.
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Published Online: 2009-9-25
Published in Print: 2002-12-1
© 2002 Oldenbourg Wissenschaftsverlag GmbH
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Articles in the same Issue
- Preface: Macromolecular Crystallography
- More power for direct methods: SIR2002
- ACORN — theory and practice
- Macromolecular phasing with SHELXE
- Physical measurement of triplet invariants: present state of the experiment, data evaluation and future perspectives
- Qantitative determination of phase for macromolecular crystals using multiple diffraction methods and dynamical theory
- Ab initio phasing starting from low resolution
- Towards automated protein structure determination: BnP, the SnB-PHASES interface
- Direct way to anomalous scatterers
- The approach of the joint probability distribution functions: the SIR-MIR, SAD-MAD and SIRAS-MIRAS, cases
- Direct-method phasing of anomalous diffraction from proteins
- Molecular replacement and high-throughput structure determination
