3QYU

Crystal structure of human cyclophilin D at 1.54 A resolution at room temperature

Summary for 3QYU

• Entry DOI: 10.2210/pdb3qyu/pdb
• Related: 3QYW 3QYZ
• Descriptor: Peptidyl-prolyl cis-trans isomerase F (2 entities in total)
• Functional Keywords: beta barrel, prolyl cis/trans isomerase, mitochondria, isomerase
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion matrix : P30405
• Total number of polymer chains: 1
• Total formula weight: 17652.13

Authors

Colliandre, L.,Gelin, M.,Labesse, G.,Guichou, J.-F. (deposition date: 2011-03-04, release date: 2011-08-24, Last modification date: 2023-09-13)

Primary citation

le Maire, A.,Gelin, M.,Pochet, S.,Hoh, F.,Pirocchi, M.,Guichou, J.F.,Ferrer, J.L.,Labesse, G.
In-plate protein crystallization, in situ ligand soaking and X-ray diffraction.
Acta Crystallogr.,Sect.D, 67:747-755, 2011

PubMed Abstract: X-ray crystallography is now a recognized technique for ligand screening, especially for fragment-based drug design. However, protein crystal handling is still tedious and limits further automation. An alternative method for the solution of crystal structures of proteins in complex with small ligands is proposed. Crystallization drops are directly exposed to an X-ray beam after cocrystallization or soaking with the desired ligands. The use of dedicated plates in connection with an optimal parametrization of the G-rob robot allows efficient data collection. Three proteins currently under study in our laboratory for ligand screening by X-ray crystallography were used as validation test cases. The protein crystals belonged to different space groups, including a challenging monoclinic case. The resulting diffraction data can lead to clear ligand recognition, including indication of alternating conformations. These results demonstrate a possible method for automation of ligand screening by X-ray crystallography.

PubMed: 21904027
DOI: 10.1107/S0907444911023249

Experimental method

X-RAY DIFFRACTION (1.54 Å)