Published in

International Union of Crystallography, Acta Crystallographica Section D: Biological Crystallography, 4(52), p. 813-825, 1996

DOI: 10.1107/s0907444996002557

Links

Tools

Export citation

Search in Google Scholar

TheAb InitioCrystal Structure Solution of Proteins by Direct Methods. VI. Complete Phasing up to Derivative Resolution

Journal article published in 1996 by C. Giacovazzo, D. Siliqi, J. Gonzalez Platas ORCID, H.-J. Hecht, G. Zanotti ORCID, B. York
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Green circle
Postprint: archiving allowed
Upload
Green circle
Published version: archiving allowed
Upload
Policy details
Data provided by SHERPA/RoMEO

Abstract

The procedure described in the papers I-V of this series [Giacovazzo, Siliqi & Ralph (1994). Acta Cryst. A50, 503-505; Giacovazzo, Siliqi & Spagna (1994). Acta Cryst. A50, 609-621; Giacovazzo, Siliqi & Zanotti (1995). Acta Cryst. A51, 177-188; Giacovazzo & Gonzalez Platas (1995). Acta Cryst. A51, 398-404; Giacovazzo, Siliqi & Gonzalez Platas (1995). Acta Cryst. A51, 811-820], aiming at estimating protein phases via a single heavy-atom derivative, has been improved so as to extend phase determination to all the reflections up to derivative resolution. The quality of the resulting electron-density maps is checked for a number of test strutures. Some of the maps are immediately interpretable, and some can be interpreted after some cycles of solvent flattening and/or histogram matching. The correlation with classical SIR techniques is also discussed.