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| Hauptseite > Publikationsdatenbank > Controlled In Meso Phase Crystallization -- A Method for the Structural Investigation of Membrane Proteins > print |
| Hauptseite > Publikationsdatenbank > Controlled In Meso Phase Crystallization -- A Method for the Structural Investigation of Membrane Proteins > print |
| 001 | 111979 | ||
| 005 | 20240610120406.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:22536388 |
| 024 | 7 | _ | |2 pmc |a pmc:PMC3334905 |
| 024 | 7 | _ | |2 DOI |a 10.1371/journal.pone.0035458 |
| 024 | 7 | _ | |2 WOS |a WOS:000305336200043 |
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| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 500 |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Kubicek, J. |b 0 |
| 245 | _ | _ | |a Controlled In Meso Phase Crystallization -- A Method for the Structural Investigation of Membrane Proteins |
| 260 | _ | _ | |a Lawrence, Kan. |b PLoS |c 2012 |
| 300 | _ | _ | |a e35458 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
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| 440 | _ | 0 | |0 18181 |a PLOS One |v 7 |x 1932-6203 |y 4 |
| 500 | _ | _ | |a Record converted from VDB: 16.11.2012 |
| 520 | _ | _ | |a We investigated in meso crystallization of membrane proteins to develop a fast screening technology which combines features of the well established classical vapor diffusion experiment with the batch meso phase crystallization, but without premixing of protein and monoolein. It inherits the advantages of both methods, namely (i) the stabilization of membrane proteins in the meso phase, (ii) the control of hydration level and additive concentration by vapor diffusion. The new technology (iii) significantly simplifies in meso crystallization experiments and allows the use of standard liquid handling robots suitable for 96 well formats. CIMP crystallization furthermore allows (iv) direct monitoring of phase transformation and crystallization events. Bacteriorhodopsin (BR) crystals of high quality and diffraction up to 1.3 Å resolution have been obtained in this approach. CIMP and the developed consumables and protocols have been successfully applied to obtain crystals of sensory rhodopsin II (SRII) from Halobacterium salinarum for the first time. |
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| 588 | _ | _ | |a Dataset connected to Pubmed |
| 650 | _ | 2 | |2 MeSH |a Bacteriorhodopsins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Crystallization |
| 650 | _ | 2 | |2 MeSH |a Crystallography, X-Ray: methods |
| 650 | _ | 2 | |2 MeSH |a Glycerides: chemistry |
| 650 | _ | 2 | |2 MeSH |a Halobacterium salinarum |
| 650 | _ | 2 | |2 MeSH |a Halorhodopsins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Membrane Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Phase Transition |
| 650 | _ | 2 | |2 MeSH |a Protein Stability |
| 650 | _ | 2 | |2 MeSH |a Sensory Rhodopsins: chemistry |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Glycerides |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Halorhodopsins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Membrane Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Sensory Rhodopsins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a sensory rhodopsin II protein, archaeal |
| 650 | _ | 7 | |0 25496-72-4 |2 NLM Chemicals |a monoolein |
| 650 | _ | 7 | |0 53026-44-1 |2 NLM Chemicals |a Bacteriorhodopsins |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Schlesinger, R. |b 1 |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB59848 |a Baeken, C. |b 2 |u FZJ |
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| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Schäfer, F. |b 4 |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB886 |a Labahn, J. |b 5 |u FZJ |
| 773 | _ | _ | |0 PERI:(DE-600)2267670-3 |a 10.1371/journal.pone.0035458 |g Vol. 7, p. e35458 |p e35458 |q 7 |v 7 |x 1932-6203 |y 2012 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3334905 |
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