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Edgar Weckert, R. Müller, J. Zellner, I. Zegers, R. Loris

Physical measurement of triplet invariants: present state of the experiment, data evaluation and future perspectives

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.

Zeitschrift für Kristallographie, Oldenbourg Wissenschaftsverlag

Print ISSN: 0044-2968
Volume: 217, 12/2002
Pages: 651

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