Optimized measurement temperature gives access to the solution structure of a 49 kDa homohexameric [beta]-propeller

The hyperthermophilic nature of the protein to minimize unfavorable relaxation properties was exploited to study the high-resolution structure of the C-terminal hexamerization domain (Ph1500C) from the hyperthermophilic archaeon Pyrococcus horikoshii. The side chain assignment (97%) and structure determination of Ph1500C which was possible at full proton density revealed Ph1500C as the largest protein.