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

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2010-10, Vol.66 (10), p.1381-1392
• Main Authors: Mohanty, Biswaranjan, Serrano, Pedro, Pedrini, Bill, Jaudzems, Kristaps, Geralt, Michael, Horst, Reto, Herrmann, Torsten, Elsliger, Marc-André, Wilson, Ian A., Wüthrich, Kurt
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; BASIC BIOLOGICAL SCIENCES; Biochemistry & Molecular Biology; Biophysics; Crystallography; Crystallography, X-Ray; Models, Molecular; Molecular Sequence Data; NMR and crystal structure comparison; NMR in a high-throughput environment; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Tertiary; reference structures; Structural Homology, Protein; structure-determination software; Thermotoga maritima; Thermotoga maritima - chemistry
• ISSN: 1744-3091; 1744-3091; 2053-230X
• DOI: 10.1107/S1744309110020956

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