Open AccessCrystallization of protein–ligand complexes
Author(s) -
Hassell Anne M.,
An Gang,
Bledsoe Randy K.,
Bynum Jane M.,
Carter H. Luke,
Deng SuJun J.,
Gampe Robert T.,
Grisard Tamara E.,
Madauss Kevin P.,
Nolte Robert T.,
Rocque Warren J.,
Wang Liping,
Weaver Kurt L.,
Williams Shawn P.,
Wisely G. Bruce,
Xu Robert,
Shewchuk Lisa M.
Publication year - 2007
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444906047020
Subject(s) - ligand (biochemistry) , protein crystallization , chemistry , crystallization , cofactor , nucleic acid , molecule , crystallography , biochemistry , enzyme , receptor , organic chemistry
Obtaining diffraction‐quality crystals has long been a bottleneck in solving the three‐dimensional structures of proteins. Often proteins may be stabilized when they are complexed with a substrate, nucleic acid, cofactor or small molecule. These ligands, on the other hand, have the potential to induce significant conformational changes to the protein and ab initio screening may be required to find a new crystal form. This paper presents an overview of strategies in the following areas for obtaining crystals of protein–ligand complexes: (i) co‐expression of the protein with the ligands of interest, (ii) use of the ligands during protein purification, (iii) cocrystallization and (iv) soaks.