Related ArticlesA NMR guided approach for CsrA-RNA crystallization.
J Biomol NMR. 2013 Jan 29;
Authors: Koharudin LM, Boelens R, Kaptein R, Gronenborn AM
Abstract
Structure determination of protein-nucleic acid complexes remains a challenging task. Here we present a simple method for generating crystals of a CsrA-nucleic acid complex, guided entirely by results from nuclear magnetic resonances spectroscopy (NMR) spectroscopy. Using a construct that lacks thirteen non-essential C-terminal residues, efficient binding to DNA could be demonstrated. One CsrA dimer interacts with two DNA oligonucleotides, similar to previous findings with RNA. Furthermore, the NMR study of the CsrA-DNA complex was the basis for successfully homing in on conditions that were suitable for obtaining crystals of the CsrA-DNA complex. Our results may be useful for those cases where RNA in protein-nucleic acid complexes may be replaced by DNA.
PMID: 23359257 [PubMed - as supplied by publisher]
Understanding Protein Crystallization Growth at the University of ... - Azom.com
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Understanding Protein Crystallization Growth at the University of Leeds using a ... Mass Spectrometers · Nuclear Magnetic Resonance Spectroscopy (NMR) ...
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06-28-2012 07:54 AM
Protein-ligand docking guided by ligand pharmacophore-mapping experiment by NMR.
Protein-ligand docking guided by ligand pharmacophore-mapping experiment by NMR.
Protein-ligand docking guided by ligand pharmacophore-mapping experiment by NMR.
J Mol Graph Model. 2011 Sep 3;
Authors: Fukunishi Y, Mizukoshi Y, Takeuchi K, Shimada I, Takahashi H, Nakamura H
Abstract
We developed a new protein-ligand docking calculation method using experimental NMR data. Recently, we proposed a novel ligand epitope-mapping experiment, which utilizes the difference between the longitudinal relaxation rates of ligand protons with and...
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09-24-2011 04:11 PM
[NMR paper] Expression, purification, crystallization, and NMR studies of the helicase interactio
Expression, purification, crystallization, and NMR studies of the helicase interaction domain of Escherichia coli DnaG primase.
Related Articles Expression, purification, crystallization, and NMR studies of the helicase interaction domain of Escherichia coli DnaG primase.
Protein Expr Purif. 2004 Feb;33(2):304-10
Authors: Loscha K, Oakley AJ, Bancia B, Schaeffer PM, Prosselkov P, Otting G, Wilce MC, Dixon NE
In Escherichia coli, the DnaG primase is the RNA polymerase that synthesizes RNA primers at replication forks. It is composed of three...
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11-24-2010 09:25 PM
[NMR paper] Purification, crystallization, NMR spectroscopy and biochemical analyses of alpha-phy
Purification, crystallization, NMR spectroscopy and biochemical analyses of alpha-phycoerythrocyanin peptides.
Related Articles Purification, crystallization, NMR spectroscopy and biochemical analyses of alpha-phycoerythrocyanin peptides.
Eur J Biochem. 2002 Oct;269(20):5046-55
Authors: Wiegand G, Parbel A, Seifert MH, Holak TA, Reuter W
The alpha-phycoerythrocyanin subunits of the different phycoerythrocyanin complexes of the phycobilisomes from the cyanobacterium Mastigocladus laminosus perform a remarkable photochemistry. Similar to...
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[NMR paper] Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectrosc
Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectroscopy.
Related Articles Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectroscopy.
Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):421-4
Authors: Vivian JP, Wilce JA, Hastings AF, Wilce MC
The replication terminator protein (RTP)-DNA complex of Bacillus subtilis is responsible for the arrest of DNA replication at terminator sites in the B. subtilis chromosome. The crystallization and preliminary diffraction data analysis...
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11-19-2010 08:32 PM
[NMR paper] Crystallization and structure solution of p53 (residues 326-356) by molecular replace
Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template.
Related Articles Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template.
Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):86-9
Authors: Mittl PR, Chčne P, Grütter MG
The molecular replacement method is a powerful technique for crystal structure solution but the use of NMR structures as templates often causes problems. In this work the NMR structure of...
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[NMR paper] Short chain phospholipids in membrane protein crystallization: a 31P-NMR study of col
Short chain phospholipids in membrane protein crystallization: a 31P-NMR study of colloidal properties of dihexanoyl phosphatidylcholine.
Related Articles Short chain phospholipids in membrane protein crystallization: a 31P-NMR study of colloidal properties of dihexanoyl phosphatidylcholine.
Chem Phys Lipids. 1990 Sep;55(3):351-4
Authors: Eisele JL, Neumann JM, Chachaty C
The colloidal features of short chain phospholipids can be deduced from 31P-NMR analysis by comparison with available data on phospholipid aqueous dispersion. In this study...