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Title: The Effect of Ionic Liquids on Protein Crystallization and X-ray Diffraction Resolution

Authors:
; ; ; ; ;  [1]
  1. (Abbott)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
INDUSTRY
OSTI Identifier:
1107392
Resource Type:
Journal Article
Resource Relation:
Journal Name: Cryst. Growth Des.; Journal Volume: 9; Journal Issue: (8) ; 08, 2009
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Judge, Russell A., Takahashi, Sumiko, Longenecker, Kenton L., Fry, Elizabeth H., Abad-Zapatero, Cele, and Chiu, Mark L. The Effect of Ionic Liquids on Protein Crystallization and X-ray Diffraction Resolution. United States: N. p., 2013. Web. doi:10.1021/cg900140b.
Judge, Russell A., Takahashi, Sumiko, Longenecker, Kenton L., Fry, Elizabeth H., Abad-Zapatero, Cele, & Chiu, Mark L. The Effect of Ionic Liquids on Protein Crystallization and X-ray Diffraction Resolution. United States. doi:10.1021/cg900140b.
Judge, Russell A., Takahashi, Sumiko, Longenecker, Kenton L., Fry, Elizabeth H., Abad-Zapatero, Cele, and Chiu, Mark L. Wed . "The Effect of Ionic Liquids on Protein Crystallization and X-ray Diffraction Resolution". United States. doi:10.1021/cg900140b.
@article{osti_1107392,
title = {The Effect of Ionic Liquids on Protein Crystallization and X-ray Diffraction Resolution},
author = {Judge, Russell A. and Takahashi, Sumiko and Longenecker, Kenton L. and Fry, Elizabeth H. and Abad-Zapatero, Cele and Chiu, Mark L.},
abstractNote = {},
doi = {10.1021/cg900140b},
journal = {Cryst. Growth Des.},
number = (8) ; 08, 2009,
volume = 9,
place = {United States},
year = {Wed Nov 20 00:00:00 EST 2013},
month = {Wed Nov 20 00:00:00 EST 2013}
}
  • Ionic liquids exhibit a variety of properties that make them attractive solvents for biomaterials. Given the potential for productive interaction between ionic liquids and biological macromolecules, we investigated the use of ionic liquids as precipitating agents and additives for protein crystallization for six model proteins (lysozyme, catalase, myoglobin, trypsin, glucose isomerase, and xylanase). The ionic liquids produced changes in crystal morphology and mediated significant increases in crystal size in some cases. Crystals grown using ionic liquids as precipitating agents or as additives provided X-ray diffraction resolution similar to or better than that obtained without ionic liquids. Based upon the experimentsmore » performed with model proteins, the ionic liquids were used as additives for the crystallization of the poorly diffracting monoclonal antibody 106.3 Fab in complex with the B-type natriuretic peptide (5-13). The ionic liquids improved the crystallization behavior and provided improved diffraction resulting in the determination of the structure. Ionic liquids should be considered as useful additives for the crystallization of other proteins.« less
  • The X-CHIP (X-ray Crystallization High-throughput Integrated Platform) is a novel microchip that has been developed to combine multiple steps of the crystallographic pipeline from crystallization to diffraction data collection on a single device to streamline the entire process. The system has been designed for crystallization condition screening, visual crystal inspection, initial X-ray screening and data collection in a high-throughput fashion. X-ray diffraction data acquisition can be performed directly on-the-chip at room temperature using an in situ approach. The capabilities of the chip eliminate the necessity for manual crystal handling and cryoprotection of crystal samples, while allowing data collection from multiplemore » crystals in the same drop. This technology would be especially beneficial for projects with large volumes of data, such as protein-complex studies and fragment-based screening. The platform employs hydrophilic and hydrophobic concentric ring surfaces on a miniature plate transparent to visible light and X-rays to create a well defined and stable microbatch crystallization environment. The results of crystallization and data-collection experiments demonstrate that high-quality well diffracting crystals can be grown and high-resolution diffraction data sets can be collected using this technology. Furthermore, the quality of a single-wavelength anomalous dispersion data set collected with the X-CHIP at room temperature was sufficient to generate interpretable electron-density maps. This technology is highly resource-efficient owing to the use of nanolitre-scale drop volumes. It does not require any modification for most in-house and synchrotron beamline systems and offers a promising opportunity for full automation of the X-ray structure-determination process.« less
  • The X-CHIP (X-ray Crystallography High-throughput Integrated Platform) is a novel microchip that has been developed to combine multiple steps of the crystallographic pipeline from crystallization to diffraction data collection on a single device to streamline the entire process. The X-CHIP (X-ray Crystallization High-throughput Integrated Platform) is a novel microchip that has been developed to combine multiple steps of the crystallographic pipeline from crystallization to diffraction data collection on a single device to streamline the entire process. The system has been designed for crystallization condition screening, visual crystal inspection, initial X-ray screening and data collection in a high-throughput fashion. X-ray diffractionmore » data acquisition can be performed directly on-the-chip at room temperature using an in situ approach. The capabilities of the chip eliminate the necessity for manual crystal handling and cryoprotection of crystal samples, while allowing data collection from multiple crystals in the same drop. This technology would be especially beneficial for projects with large volumes of data, such as protein-complex studies and fragment-based screening. The platform employs hydrophilic and hydrophobic concentric ring surfaces on a miniature plate transparent to visible light and X-rays to create a well defined and stable microbatch crystallization environment. The results of crystallization and data-collection experiments demonstrate that high-quality well diffracting crystals can be grown and high-resolution diffraction data sets can be collected using this technology. Furthermore, the quality of a single-wavelength anomalous dispersion data set collected with the X-CHIP at room temperature was sufficient to generate interpretable electron-density maps. This technology is highly resource-efficient owing to the use of nanolitre-scale drop volumes. It does not require any modification for most in-house and synchrotron beamline systems and offers a promising opportunity for full automation of the X-ray structure-determination process.« less
  • No abstract prepared.
  • Hemextin A was isolated and purified from African Ringhals cobra (Hemachatus haemachatus). It is a three-finger toxin that specifically inhibits blood coagulation factor VIIa and clot formation and that also interacts with hemextin B to form a unique anticoagulant complex. Hemextin A was crystallized by the hanging-drop vapor-diffusion method by equilibration against 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate pH 4.6 and 30% PEG 4000 as the precipitating agent. The crystals belong to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 49.27, b = 49.51, c = 57.87 {angstrom} and two molecules in the asymmetricmore » unit. They diffracted to 1.5 {angstrom} resolution at beamline X25 at BNL.« less