Structural basis for mobility in the 1.1 Å crystal structure of the NG domain of Thermus aquaticus Ffh

INIS

• interfaces 100%
• signals 100%
• interactions 66%
• proteins 66%
• dynamics 66%
• mobility 66%
• data 33%
• resolution 33%
• orientation 33%
• particles 33%
• receptors 33%
• membranes 33%
• nucleotides 33%
• anisotropy 33%
• residues 33%
• packing 33%
• crystal structure 33%

Biochemistry, Genetics and Molecular Biology

• GTPase 100%
• Thermus aquaticus 66%
• Protein 66%
• Dynamics 66%
• Membrane 33%
• Crystal Structure 33%
• Nucleotide 33%
• Conserved Sequence 33%
• Recognition Sequence 33%
• Signal Recognition Particle 33%
• Sequence Motif 33%
• Interpersonal Communication 33%
• Recognition 33%