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| | <StructureSection load='5v33' size='340' side='right'caption='[[5v33]], [[Resolution|resolution]] 3.49Å' scene=''> | | <StructureSection load='5v33' size='340' side='right'caption='[[5v33]], [[Resolution|resolution]] 3.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5v33]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V33 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V33 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5v33]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V33 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.487Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">puhA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907]), pufL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907]), pufM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5v33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v33 OCA], [http://pdbe.org/5v33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v33 RCSB], [http://www.ebi.ac.uk/pdbsum/5v33 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v33 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5v33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v33 OCA], [https://pdbe.org/5v33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v33 RCSB], [https://www.ebi.ac.uk/pdbsum/5v33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v33 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RCEH_RHOSH RCEH_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/RCEM_RHOSH RCEM_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/RCEL_RHOSH RCEL_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. | + | [https://www.uniprot.org/uniprot/RCEH_CERSP RCEH_CERSP] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rhodococcus capsulatus molisch 1907]] | + | [[Category: Cereibacter sphaeroides]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Broecker, J]] | + | [[Category: Broecker J]] |
| - | [[Category: Ernst, O P]] | + | [[Category: Ernst OP]] |
| - | [[Category: Gennis, R B]] | + | [[Category: Gennis RB]] |
| - | [[Category: Kenis, P J.A]] | + | [[Category: Kenis PJA]] |
| - | [[Category: Pawate, A S]] | + | [[Category: Pawate AS]] |
| - | [[Category: Schieferstein, J M]] | + | [[Category: Schieferstein JM]] |
| - | [[Category: Sun, C]] | + | [[Category: Sun C]] |
| - | [[Category: Wan, F]] | + | [[Category: Wan F]] |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Reaction center mutant]]
| + | |
| Structural highlights
Function
RCEH_CERSP The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
Publication Abstract from PubMed
Elucidating and clarifying the function of membrane proteins ultimately requires atomic resolution structures as determined most commonly by X-ray crystallography. Many high impact membrane protein structures have resulted from advanced techniques such as in meso crystallization that present technical difficulties for the set-up and scale-out of high-throughput crystallization experiments. In prior work, we designed a novel, low-throughput X-ray transparent microfluidic device that automated the mixing of protein and lipid by diffusion for in meso crystallization trials. Here, we report X-ray transparent microfluidic devices for high-throughput crystallization screening and optimization that overcome the limitations of scale and demonstrate their application to the crystallization of several membrane proteins. Two complementary chips are presented: (1) a high-throughput screening chip to test 192 crystallization conditions in parallel using as little as 8 nl of membrane protein per well and (2) a crystallization optimization chip to rapidly optimize preliminary crystallization hits through fine-gradient re-screening. We screened three membrane proteins for new in meso crystallization conditions, identifying several preliminary hits that we tested for X-ray diffraction quality. Further, we identified and optimized the crystallization condition for a photosynthetic reaction center mutant and solved its structure to a resolution of 3.5 A.
X-ray transparent microfluidic chips for high-throughput screening and optimization of in meso membrane protein crystallization.,Schieferstein JM, Pawate AS, Sun C, Wan F, Sheraden PN, Broecker J, Ernst OP, Gennis RB, Kenis PJA Biomicrofluidics. 2017 Apr 24;11(2):024118. doi: 10.1063/1.4981818. eCollection, 2017 Mar. PMID:28469762[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schieferstein JM, Pawate AS, Sun C, Wan F, Sheraden PN, Broecker J, Ernst OP, Gennis RB, Kenis PJA. X-ray transparent microfluidic chips for high-throughput screening and optimization of in meso membrane protein crystallization. Biomicrofluidics. 2017 Apr 24;11(2):024118. doi: 10.1063/1.4981818. eCollection, 2017 Mar. PMID:28469762 doi:http://dx.doi.org/10.1063/1.4981818
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