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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Autores principales:	Jan Kubicek, Ramona Schlesinger, Christian Baeken, Georg Büldt, Frank Schäfer, Jörg Labahn
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/21562b19775e41b18c761a10724f1f49
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spelling	oai:doaj.org-article:21562b19775e41b18c761a10724f1f492021-11-18T07:21:36ZControlled in meso phase crystallization--a method for the structural investigation of membrane proteins.1932-620310.1371/journal.pone.0035458https://doaj.org/article/21562b19775e41b18c761a10724f1f492012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22536388/?tool=EBIhttps://doaj.org/toc/1932-6203We 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.Jan KubicekRamona SchlesingerChristian BaekenGeorg BüldtFrank SchäferJörg LabahnPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 4, p e35458 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jan Kubicek Ramona Schlesinger Christian Baeken Georg Büldt Frank Schäfer Jörg Labahn Controlled in meso phase crystallization--a method for the structural investigation of membrane proteins.
description	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.
format	article
author	Jan Kubicek Ramona Schlesinger Christian Baeken Georg Büldt Frank Schäfer Jörg Labahn
author_facet	Jan Kubicek Ramona Schlesinger Christian Baeken Georg Büldt Frank Schäfer Jörg Labahn
author_sort	Jan Kubicek
title	Controlled in meso phase crystallization--a method for the structural investigation of membrane proteins.
title_short	Controlled in meso phase crystallization--a method for the structural investigation of membrane proteins.
title_full	Controlled in meso phase crystallization--a method for the structural investigation of membrane proteins.
title_fullStr	Controlled in meso phase crystallization--a method for the structural investigation of membrane proteins.
title_full_unstemmed	Controlled in meso phase crystallization--a method for the structural investigation of membrane proteins.
title_sort	controlled in meso phase crystallization--a method for the structural investigation of membrane proteins.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/21562b19775e41b18c761a10724f1f49
work_keys_str_mv	AT jankubicek controlledinmesophasecrystallizationamethodforthestructuralinvestigationofmembraneproteins AT ramonaschlesinger controlledinmesophasecrystallizationamethodforthestructuralinvestigationofmembraneproteins AT christianbaeken controlledinmesophasecrystallizationamethodforthestructuralinvestigationofmembraneproteins AT georgbuldt controlledinmesophasecrystallizationamethodforthestructuralinvestigationofmembraneproteins AT frankschafer controlledinmesophasecrystallizationamethodforthestructuralinvestigationofmembraneproteins AT jorglabahn controlledinmesophasecrystallizationamethodforthestructuralinvestigationofmembraneproteins
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Controlled in meso phase crystallization--a method for the structural investigation of membrane proteins.

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