CRYSTAL STRUCTURE OF THE HYBRID C-TERMINAL DOMAIN OF ENZYME I OF THE BACTERIAL PHOSPHOTRANSFERASE SYSTEM FORMED BY HYBRIDIZING THE SCAFFOLD OF THE ESCHERICHIA COLI ENZYME WITH THE ACTIVE SITE LOOPS FROM THE THERMOANAEROBACTER TENGCONGENSIS ENZYME

2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.

1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.

Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I.

Phosphoenolpyruvate-protein phosphotransferase

0.2 M Magnesium chloride hexahydrate, 0.1 M HEPES pH 7.0 and 20% w/v PEG 6000

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

Phosphoenolpyruvate-protein phosphotransferase (E.C.2.7.3.9)

phosphoenolpyruvate-protein phosphotransferase PtsI, Hybrid, bacterial phosphotransferase, TRANSFERASE