Oxford Univ Press / Protein Data Bank / Global Phasing Ltd / Short SA / Amersham / Ligand / C-6 OH / mCi / Qiagen / Storoni LC / Cell / Weinglass AB / Schrödinger LLC / /
Country
Germany / Hungary / United Kingdom / /
Currency
pence / / /
Facility
bMolecular Biology Institute / C terminus / cHoward Hughes Medical Institute / University of Pécs / LacY complex / Texas Tech University Health Sciences Center / University of California / /
IndustryTerm
substrate-binding site / free energy / reagents/analytic tools / sugar binding site / macromolecular structure solution / crystallization solutions / energy coupling / sugar-binding site / reservoir solution / search models / /
MusicGroup
Cell / /
Organization
National Science Foundation / Abramson / Abramson and Kaback / cHoward Hughes Medical Institute / Department of Chemistry / bMolecular Biology Institute / Department of Physiology / Texas Tech University Health Sciences Center / University of California / Los Angeles / David Geffen School of Medicine / University of Pécs / GM074929 / Republicans / /
Person
Facilitator Superfamily / Michael R. Sawayab / Van Iwaarden / Coot / Carter / Jr / H. Ronald Kaback / H. Ronald Kabacka / Vincent Chaptala / Tomás Kalai / Jeff Abramsona / /
Position
Author / Major / intensively studied representative / Model / /
Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition Vincent Chaptala, Seunghyug Kwona, Michael R. Sawayab,c, Lan Guand, H. Ronald Kabacka,e,1, and Je