Related ArticlesPreliminary X-ray crystallographic and NMR studies on the exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III.
J Struct Biol. 2000 Aug;131(2):164-9
Authors: Hamdan S, Brown SE, Thompson PR, Yang JY, Carr PD, Ollis DL, Otting G, Dixon NE
The structured core of the N-terminal 3'-5' exonuclease domain of epsilon, the proofreading subunit of Escherichia coli DNA polymerase III, was defined by multidimensional NMR experiments with uniformly (15)N-labeled protein: it comprises residues between Ile-4 and Gln-181. A 185-residue fragment, termed epsilon(1-185), was crystallized by the hanging drop vapor diffusion method in the presence of thymidine-5'-monophosphate, a product inhibitor, and Mn(2+) at pH 5.8. The crystals are tetragonal, with typical dimensions 0.2 mm x 0.2 mm x 1.0 mm, grow over about 2 weeks at 4 degrees C, and diffract X-rays to 2.0 A. The space group was determined to be P4(n)2(1)2 (n = 0, 1, 2, 3), with unit cell dimensions a = 60.8 A, c = 111.4 A.
[NMR paper] Crystallographic and NMR investigation of cobalt-substituted amicyanin.
Crystallographic and NMR investigation of cobalt-substituted amicyanin.
Related Articles Crystallographic and NMR investigation of cobalt-substituted amicyanin.
Biochemistry. 2004 Jul 27;43(29):9381-9
Authors: Carrell CJ, Wang X, Jones L, Jarrett WL, Davidson VL, Mathews FS
Cobalt(II) amicyanin was prepared by replacing the copper of the type I copper protein amicyanin from Paracoccus denitrificans with cobalt. The structure of the protein and the metal center have been characterized by X-ray crystallography and paramagnetic NMR spectroscopy....
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[NMR paper] Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interact
Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD.
Related Articles Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD.
Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):709-14
Authors: Bann JG, Pinkner J, Hultgren SJ, Frieden C
PapD is a periplasmic chaperone essential for P pilus formation in pyelonephritic strains of E. coli. It is composed of two domains, each of which contains a tryptophan...
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[NMR paper] Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in
Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli.
FEBS Lett. 1997 Sep 29;415(2):155-9
Authors: Davydova NL, Rak AV, Gryaznova OI, Liljas A, Jonsson BH, Berglund H, Härd T, Garber MB
The gene for the ribosomal protein S19 from Thermus thermophilus was cloned,...
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[NMR paper] NMR, molecular modeling, and crystallographic studies of lentil lectin-sucrose intera
NMR, molecular modeling, and crystallographic studies of lentil lectin-sucrose interaction.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR, molecular modeling, and crystallographic studies of lentil lectin-sucrose interaction.
J Biol Chem. 1995 Oct 27;270(43):25619-28
Authors: Casset F, Hamelryck T, Loris R, Brisson JR, Tellier C, Dao-Thi MH, Wyns L, Poortmans F, Pérez S, Imberty A
The conformational features of sucrose in the...
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[NMR paper] Purification of cloned trypanosomal calmodulin and preliminary NMR studies.
Purification of cloned trypanosomal calmodulin and preliminary NMR studies.
Related Articles Purification of cloned trypanosomal calmodulin and preliminary NMR studies.
J Chromatogr. 1991 Feb 22;539(2):501-5
Authors: Sweeney PJ, Walker JM, Reid DG, Elshourbagy N
Cloned trypanosomal calmodulin was expressed in Escherichia coli and purified to homogeneity using hydrophobic interaction chromatography on phenyl-Sepharose. The purified protein was subjected to NMR analysis which allows detailed changes to be observed when, firstly, calcium, and...
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[NMR paper] 1H and 15N NMR resonance assignments and preliminary structural characterization of E
1H and 15N NMR resonance assignments and preliminary structural characterization of Escherichia coli apocytochrome b562.
Related Articles 1H and 15N NMR resonance assignments and preliminary structural characterization of Escherichia coli apocytochrome b562.
Biochemistry. 1991 Aug 6;30(31):7711-7
Authors: Feng YQ, Wand AJ, Sligar SG
The 1H and 15N resonances of uniformly enriched apocytochrome b562 (106 residues) have been assigned. The assignment work began with the identification of the majority of HN-H alpha-H beta subspin systems in...
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[NMR paper] 1H and 15N NMR resonance assignments and preliminary structural characterization of E
1H and 15N NMR resonance assignments and preliminary structural characterization of Escherichia coli apocytochrome b562.
Related Articles 1H and 15N NMR resonance assignments and preliminary structural characterization of Escherichia coli apocytochrome b562.
Biochemistry. 1991 Aug 6;30(31):7711-7
Authors: Feng YQ, Wand AJ, Sligar SG
The 1H and 15N resonances of uniformly enriched apocytochrome b562 (106 residues) have been assigned. The assignment work began with the identification of the majority of HN-H alpha-H beta subspin systems in...
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[NMR paper] 1H NMR studies on bovine cyclophilin: preliminary structural characterization of its
1H NMR studies on bovine cyclophilin: preliminary structural characterization of its complex with cyclosporin A.
Related Articles 1H NMR studies on bovine cyclophilin: preliminary structural characterization of its complex with cyclosporin A.
Biochemistry. 1990 May 8;29(18):4466-78
Authors: Heald SL, Harding MW, Handschumacher RE, Armitage IM
Cyclophilin (163 residues, Mr 17737), a peptidyl prolyl cis-trans isomerase, is a cytosolic protein that specifically binds the potent immunosuppressant cyclosporin A (CsA). The native form of the major...