This title appears in the Scientific Report :
2012
Please use the identifier:
http://dx.doi.org/10.1371/journal.pone.0035458 in citations.
Please use the identifier: http://hdl.handle.net/2128/7812 in citations.
Controlled In Meso Phase Crystallization -- A Method for the Structural Investigation of Membrane Proteins
Controlled In Meso Phase Crystallization -- A Method for the Structural Investigation of Membrane Proteins
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 advantag...
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Personal Name(s): | Kubicek, J. |
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Schlesinger, R. / Baeken, C. / Büldt, G. / Schäfer, F. / Labahn, J. | |
Contributing Institute: |
Molekulare Biophysik; ICS-5 Strukturbiochemie; ICS-6 |
Published in: | PLoS one, 7 (2012) S. e35458 |
Imprint: |
Lawrence, Kan.
PLoS
2012
|
Physical Description: |
e35458 |
DOI: |
10.1371/journal.pone.0035458 |
PubMed ID: |
22536388 |
Document Type: |
Journal Article |
Research Program: |
Funktion und Dysfunktion des Nervensystems BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |
Series Title: |
PLOS One
7 |
Subject (ZB): | |
Link: |
Get full text OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/7812 in citations.
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. |