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3L0F

High resolution structure of C-Phycocyanin from Thermosynechococcus elongatus

Summary for 3L0F
Entry DOI10.2210/pdb3l0f/pdb
Related1F99 1JB0 1KTP 1PHN 2BV8 3BRP
DescriptorC-phycocyanin alpha chain, C-phycocyanin beta chain, PHYCOCYANOBILIN, ... (4 entities in total)
Functional Keywordsphotosynthesis, photosystem ii, light harvesting proteins, thermostability, bile pigment, chloroplast, chromophore, electron transport, membrane, phycobilisome, plastid, thylakoid, transport, methylation
Biological sourceThermosynechococcus elongatus
More
Cellular locationCellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P50032 P50033
Total number of polymer chains2
Total formula weight37439.36
Authors
Fromme, R.,Brune, D.,Fromme, P. (deposition date: 2009-12-09, release date: 2010-12-29, Last modification date: 2023-09-20)
Primary citationFromme, R.,Ishchenko, A.,Metz, M.,Chowdhury, S.R.,Basu, S.,Boutet, S.,Fromme, P.,White, T.A.,Barty, A.,Spence, J.C.,Weierstall, U.,Liu, W.,Cherezov, V.
Serial femtosecond crystallography of soluble proteins in lipidic cubic phase.
Iucrj, 2:545-551, 2015
Cited by
PubMed Abstract: Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) enables high-resolution protein structure determination using micrometre-sized crystals at room temperature with minimal effects from radiation damage. SFX requires a steady supply of microcrystals intersecting the XFEL beam at random orientations. An LCP-SFX method has recently been introduced in which microcrystals of membrane proteins are grown and delivered for SFX data collection inside a gel-like membrane-mimetic matrix, known as lipidic cubic phase (LCP), using a special LCP microextrusion injector. Here, it is demonstrated that LCP can also be used as a suitable carrier medium for microcrystals of soluble proteins, enabling a dramatic reduction in the amount of crystallized protein required for data collection compared with crystals delivered by liquid injectors. High-quality LCP-SFX data sets were collected for two soluble proteins, lysozyme and phycocyanin, using less than 0.1 mg of each protein.
PubMed: 26306196
DOI: 10.1107/S2052252515013160
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.35 Å)
Structure validation

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