ArticlePloS one2012
Controlled in meso phase crystallization--a method for the structural investigation of membrane proteins.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- X-ray transparent microfluidic chips for high-throughput screening and optimization ofBiomicrofluidics · 2017Article
- Stray light correction in the optical spectroscopy of crystals.Applied spectroscopy · 2015Article
- X-ray Transparent Microfluidic Chip for Mesophase-Based Crystallization of Membrane Proteins and On-Chip Structure Determination.Crystal growth & design · 2014Article
- Surfactant bilayers maintain transmembrane protein activity.Biophysical journal · 2014Article
- Effects of detergent β-octylglucoside and phosphate salt solutions on phase behavior of monoolein mesophases.Biophysical journal · 2013Article
- An overview of biological macromolecule crystallization.International journal of molecular sciences · 2013Review
- Membrane protein structure determination using crystallography and lipidic mesophases: recent advances and successes.Biochemistry · 2012Article
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Authors and funding
6 authors.
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Abstract
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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