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Title: Protein Crystal Growth in Gels and Stationary Magnetic Fields

Abstract

Thaumatin, lysozyme, and ferritin single crystals were grown in solutions and gels without and with surrounding strong stationary magnetic fields. The crystal size, number and alignment in dependence on the induction force were analyzed. The crystal quality, like mosaicity, as function of the magnetic force is discussed by using synchrotron X-ray diffraction analysis.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
929849
Report Number(s):
BNL-80414-2008-JA
Journal ID: ISSN 0232-1300; CRTEDF; TRN: US0806656
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Crystal Research and Technology; Journal Volume: 42; Journal Issue: 3
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; 43 PARTICLE ACCELERATORS; CRYSTAL GROWTH; CRYSTALS; CRYSTAL STRUCTURE; FERRITIN; GELS; INDUCTION; LYSOZYME; MAGNETIC FIELDS; MONOCRYSTALS; PROTEINS; SIZE; SOLUTIONS; SYNCHROTRON RADIATION; X-RAY DIFFRACTION; national synchrotron light source

Citation Formats

Moreno,A., Quiroz-Garcia, B., Yokaichiya, F., Stojanoff, V., and Rudolph, P. Protein Crystal Growth in Gels and Stationary Magnetic Fields. United States: N. p., 2007. Web. doi:10.1002/crat.200610805.
Moreno,A., Quiroz-Garcia, B., Yokaichiya, F., Stojanoff, V., & Rudolph, P. Protein Crystal Growth in Gels and Stationary Magnetic Fields. United States. doi:10.1002/crat.200610805.
Moreno,A., Quiroz-Garcia, B., Yokaichiya, F., Stojanoff, V., and Rudolph, P. Mon . "Protein Crystal Growth in Gels and Stationary Magnetic Fields". United States. doi:10.1002/crat.200610805.
@article{osti_929849,
title = {Protein Crystal Growth in Gels and Stationary Magnetic Fields},
author = {Moreno,A. and Quiroz-Garcia, B. and Yokaichiya, F. and Stojanoff, V. and Rudolph, P.},
abstractNote = {Thaumatin, lysozyme, and ferritin single crystals were grown in solutions and gels without and with surrounding strong stationary magnetic fields. The crystal size, number and alignment in dependence on the induction force were analyzed. The crystal quality, like mosaicity, as function of the magnetic force is discussed by using synchrotron X-ray diffraction analysis.},
doi = {10.1002/crat.200610805},
journal = {Crystal Research and Technology},
number = 3,
volume = 42,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}
  • Here, in this contribution we use nonconventional methods that help to increase the success rate of a protein crystal growth, and consequently of structural projects using X-ray diffraction techniques. In order to achieve this purpose, this contribution presents new approaches involving more sophisticated techniques of protein crystallization, not just for growing protein crystals of different sizes by using electric fields, but also for controlling crystal size and orientation. Also, this latter was possible through the use of magnetic fields that allow to obtain protein crystals suitable for both high-resolution X-ray and neutron diffraction crystallography where big crystals are required. Thismore » contribution discusses some pros, cons and realities of the role of electromagnetic fields in protein crystallization research, and their effect on protein crystal contacts. Additionally, we discuss the importance of room and low temperatures during data collection. Finally, we also discuss the effect of applying a rather strong magnetic field of 16.5 T, for shorts and long periods of time, on protein crystal growth, and on the 3D structure of two model proteins.« less
  • Survival E (SurE) protein from Campylobacter jejuni, a Gram-negative mesophile, has been overexpressed in Escherichia coli as a soluble protein, successfully purified and crystallized in two distinct crystal forms. Survival E (SurE) protein from Campylobacter jejuni, a Gram-negative mesophile, has been overexpressed in Escherichia coli as a soluble protein, successfully purified and crystallized in two distinct crystal forms. The first form belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with a tetramer in the asymmetric unit and unit-cell parameters a = 80.5, b = 119.0, c = 135.3 Å. The second form belongs to space group C2, with unit-cell parametersmore » a = 121.4, b = 47.1, c = 97.8 Å, and contains a dimer in the asymmetric unit. Diffraction data have been collected from these crystal forms to 2.5 and 2.95 Å resolution, respectively.« less
  • Earlier studies have shown that a static electric field across a capillary column increased the apparent capacity ratio (measured from the peak maximum) of a liquid crystal stationary phase and produced a more nearly Gaussian-shaped peak plus a small step on the front of the peak. The present study has qualitatively confirmed those effects using cholesteryl laurate, cholesteryl 10-undecenoate, and cholesteryl benzoate, and suggests that they may be found for all cholesteric liquid phases. In addition, the peak-fronting phenomenon was found to be a function of both the carrier gas and the applied column potential. Fragmentation of the solute and/ormore » the stationary phase by carrier gas molecules in metastable excited states is proposed to explain the fronting phenomenon. Hysteresis effects have also been observed, indicating that the liquid crystals may take hours to return to their original orientations after imposition or removal of an electric field. 4 tables, 8 figures.« less