Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4NC3

Crystal structure of the 5-HT2B receptor solved using serial femtosecond crystallography in lipidic cubic phase.

Summary for 4NC3
Entry DOI10.2210/pdb4nc3/pdb
Related4IB4
DescriptorChimera protein of human 5-hydroxytryptamine receptor 2B and E. Coli soluble cytochrome b562, PALMITIC ACID, Ergotamine, ... (10 entities in total)
Functional Keywordsserial femtosecond crystallography, human 5ht2b receptor, ergotamine, novel protein engineering, gpcr network, membrane protein, lipidic cubic phase, psi-biology, free electron laser, structural genomics, gpcr, membrane, signaling protein, electron transport
Biological sourceHomo sapiens (Human)
More
Cellular locationCell membrane ; Multi- pass membrane protein : P41595
Total number of polymer chains1
Total formula weight53259.85
Authors
Primary citationLiu, W.,Wacker, D.,Gati, C.,Han, G.W.,James, D.,Wang, D.,Nelson, G.,Weierstall, U.,Katritch, V.,Barty, A.,Zatsepin, N.A.,Li, D.,Messerschmidt, M.,Boutet, S.,Williams, G.J.,Koglin, J.E.,Seibert, M.M.,Wang, C.,Shah, S.T.,Basu, S.,Fromme, R.,Kupitz, C.,Rendek, K.N.,Grotjohann, I.,Fromme, P.,Kirian, R.A.,Beyerlein, K.R.,White, T.A.,Chapman, H.N.,Caffrey, M.,Spence, J.C.,Stevens, R.C.,Cherezov, V.
Serial femtosecond crystallography of G protein-coupled receptors.
Science, 342:1521-1524, 2013
Cited by
PubMed Abstract: X-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment.
PubMed: 24357322
DOI: 10.1126/science.1244142
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon