Structure and catalytic mechanism of the evolutionarily unique bacterial chalcone isomerase.

Thomsen M, Tuukkanen A, Dickerhoff J, Palm GJ, Kratzat H, Svergun DI, Weisz K, Bornscheuer UT, Hinrichs W
Acta Crystallogr D Biol Crystallogr 71(Pt 4):907-17 (2015 Apr)

PMID: 25849401 doi: 10.1107/S1399004715001935

Submitted to SASBDB: 2015 Jul 21 Published in SASBDB: 2017 Nov 6

SASDAL6 – Wild-type chalcone isomerase, ligand-free Sample: Bacterial chalcone isomerase hexamer, 194 kDa Eubacterium ramulus protein Buffer: 50 mM sodium phosphate, pH: 6.8 Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23 RgGuinier 4.0 nm Dmax 13.0 nm VolumePorod 320 nm3

SASDAM6 – Naringenin-bound chalcone isomerase Sample: Chalcone isomerase with Naringenin hexamer, 194 kDa Eubacterium ramulus protein Buffer: 50 mM sodium phosphate, pH: 6.8 Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23 RgGuinier 3.7 nm Dmax 11.0 nm VolumePorod 320 nm3

SASDAN6 – Chalcone isomerase, CHI_Δlid construct Sample: Chalcone isomerase deltaLid hexamer, 181 kDa Eubacterium ramulus protein Buffer: 50 mM sodium phosphate, pH: 6.8 Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23 RgGuinier 3.6 nm Dmax 11.0 nm VolumePorod 270 nm3