2i5n
From Proteopedia
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| - | [[Image:2i5n.gif|left|200px]] | + | [[Image:2i5n.gif|left|200px]] |
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| - | '''1.96 A X-ray structure of photosynthetic reaction center from Rhodopseudomonas viridis:Crystals grown by microfluidic technique''' | + | {{Structure |
| + | |PDB= 2i5n |SIZE=350|CAPTION= <scene name='initialview01'>2i5n</scene>, resolution 1.96Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=BCB:BACTERIOCHLOROPHYLL+B'>BCB</scene>, <scene name='pdbligand=BPB:BACTERIOPHEOPHYTIN+B'>BPB</scene>, <scene name='pdbligand=MQ9:MENAQUINONE-9'>MQ9</scene>, <scene name='pdbligand=UQ1:UBIQUINONE-1'>UQ1</scene>, <scene name='pdbligand=NS5:DIHYDRO-NEUROSPORENE'>NS5</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene> and <scene name='pdbligand=UNL:'>UNL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''1.96 A X-ray structure of photosynthetic reaction center from Rhodopseudomonas viridis:Crystals grown by microfluidic technique''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2I5N is a [ | + | 2I5N is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I5N OCA]. |
==Reference== | ==Reference== | ||
| - | Nanoliter microfluidic hybrid method for simultaneous screening and optimization validated with crystallization of membrane proteins., Li L, Mustafi D, Fu Q, Tereshko V, Chen DL, Tice JD, Ismagilov RF, Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19243-8. Epub 2006 Dec 11. PMID:[http:// | + | Nanoliter microfluidic hybrid method for simultaneous screening and optimization validated with crystallization of membrane proteins., Li L, Mustafi D, Fu Q, Tereshko V, Chen DL, Tice JD, Ismagilov RF, Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19243-8. Epub 2006 Dec 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17159147 17159147] |
[[Category: Blastochloris viridis]] | [[Category: Blastochloris viridis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: secondary quinone (qb)]] | [[Category: secondary quinone (qb)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:25:43 2008'' |
Revision as of 15:25, 20 March 2008
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| , resolution 1.96Å | |||||||
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| Ligands: | , , , , , , , , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
1.96 A X-ray structure of photosynthetic reaction center from Rhodopseudomonas viridis:Crystals grown by microfluidic technique
Overview
High-throughput screening and optimization experiments are critical to a number of fields, including chemistry and structural and molecular biology. The separation of these two steps may introduce false negatives and a time delay between initial screening and subsequent optimization. Although a hybrid method combining both steps may address these problems, miniaturization is required to minimize sample consumption. This article reports a "hybrid" droplet-based microfluidic approach that combines the steps of screening and optimization into one simple experiment and uses nanoliter-sized plugs to minimize sample consumption. Many distinct reagents were sequentially introduced as approximately 140-nl plugs into a microfluidic device and combined with a substrate and a diluting buffer. Tests were conducted in approximately 10-nl plugs containing different concentrations of a reagent. Methods were developed to form plugs of controlled concentrations, index concentrations, and incubate thousands of plugs inexpensively and without evaporation. To validate the hybrid method and demonstrate its applicability to challenging problems, crystallization of model membrane proteins and handling of solutions of detergents and viscous precipitants were demonstrated. By using 10 microl of protein solution, approximately 1,300 crystallization trials were set up within 20 min by one researcher. This method was compatible with growth, manipulation, and extraction of high-quality crystals of membrane proteins, demonstrated by obtaining high-resolution diffraction images and solving a crystal structure. This robust method requires inexpensive equipment and supplies, should be especially suitable for use in individual laboratories, and could find applications in a number of areas that require chemical, biochemical, and biological screening and optimization.
About this Structure
2I5N is a Protein complex structure of sequences from Blastochloris viridis. Full crystallographic information is available from OCA.
Reference
Nanoliter microfluidic hybrid method for simultaneous screening and optimization validated with crystallization of membrane proteins., Li L, Mustafi D, Fu Q, Tereshko V, Chen DL, Tice JD, Ismagilov RF, Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19243-8. Epub 2006 Dec 11. PMID:17159147
Page seeded by OCA on Thu Mar 20 17:25:43 2008
Categories: Blastochloris viridis | Protein complex | Chen, D L. | Fu, Q. | Ismagilov, R F. | Li, L. | Mustafi, D. | Tereshko, V. | Tice, J D. | BCB | BPB | FE2 | HEC | HTO | LDA | MQ9 | NS5 | SO4 | UNL | UQ1 | Hybrid | Microbatch | Microfluidic technique | Photosynthetic reaction center | Plug | Secondary quinone (qb)
