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Comparison of NMR and crystal structures for the proteins TM1112 and TM1367

Authors :
Torsten Herrmann
Marc-André Elsliger
Biswaranjan Mohanty
Bill Pedrini
Ian A. Wilson
Reto Horst
Pedro Serrano
Kurt Wüthrich
Kristaps Jaudzems
Michael Geralt
Source :
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66 (10), Acta Crystallographica Section F
Publication Year :
2010
Publisher :
International Union of Crystallography (IUCr), 2010.

Abstract

The NMR structures of the TM1112 and TM1367 proteins from Thermotoga maritima in solution at 298 K were determined following a new protocol which uses the software package UNIO for extensive automation. The results obtained with this novel procedure were evaluated by comparison with the crystal structures solved by the JCSG at 100 K to 1.83 and 1.90 Å resolution, respectively. In addition, the TM1112 solution structure was compared with an NMR structure solved by the NESG using a conventional largely interactive methodology. For both proteins, the newly determined NMR structure could be superimposed with the crystal structure with r.m.s.d. values of<br />Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66 (10)<br />ISSN:1744-3091<br />ISSN:2053-230X

Details

ISSN :
17443091 and 2053230X
Volume :
66
Database :
OpenAIRE
Journal :
Acta Crystallographica Section F Structural Biology and Crystallization Communications
Accession number :
edsair.doi.dedup.....8e93ab383ecdf4daa517e4db1ba2a3b5
Full Text :
https://doi.org/10.1107/s1744309110020956