After a structure calculation with the aria 2.2 software I used aqua and procheck_nmr to assess the result. Although procheck_nmr worked fine on my 20 refined structures (in aria’s refine directory), it ran into trouble with the 100 structures after iteration 8 (directory it8): * Restraints read in from file: * allpdb.nrv [...]
[NMR paper] Improving the accuracy of NMR structures of large proteins using pseudocontact shifts
Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints.
Related Articles Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints.
J Biomol NMR. 2004 Mar;28(3):205-12
Authors: Gaponenko V, Sarma SP, Altieri AS, Horita DA, Li J, Byrd RA
We demonstrate improved accuracy in protein structure determination for large (>/=30 kDa), deuterated proteins (e.g. STAT4(NT)) via the combination of pseudocontact shifts for amide and methyl protons...
nmrlearner
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11-24-2010 09:25 PM
[NMR paper] TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution
TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution.
Related Articles TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution.
Trends Biochem Sci. 2000 Oct;25(10):462-8
Authors: Riek R, Pervushin K, Wüthrich K
TROSY and CRINEPT are new techniques for solution NMR studies of molecular and supramolecular structures. They allow the collection of high-resolution spectra of structures with molecular weights >100 kDa, significantly extending the range of macromolecular systems that can...
nmrlearner
Journal club
0
11-19-2010 08:29 PM
[NMR paper] Determining the structures of large proteins and protein complexes by NMR.
Determining the structures of large proteins and protein complexes by NMR.
Related Articles Determining the structures of large proteins and protein complexes by NMR.
Trends Biotechnol. 1998 Jan;16(1):22-34
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional NMR methodology to obtain 1H, 15N and 13C resonance assignments, interproton-distance and torsion-angle restraints, and restraints that characterize long-range order have, coupled with new methods of structure refinement, permitted solution structure of proteins in excess...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
peak intensity vs number of scans
Hi,
I have a question regarding how the peak intensities change when with increase in number of scans when the data is collected on a Varian NMR spectrometer. Suppose I collect a 15N-1H HSQC spectra with 8 scans and then collect the same spectra with 16 scans, would the peak intensities be double in the 16 scan spectra as compared to the 8 scan spectra? Does anyone know how the varian spectrometer scales the intensities according to the number of scans? Any suggestion or reply to my query will be extremely useful and greatly appreciated.
Thanks.
aish1982
NMR software
0
08-08-2008 11:56 PM
peak intensity vs number of scans
Hi,
I have a question regarding how the peak intensities change when with increase in number of scans when the data is collected on a Varian NMR spectrometer. Suppose I collect a 15N-1H HSQC spectra with 8 scans and then collect the same spectra with 16 scans, would the peak intensities be double in the 16 scan spectra as compared to the 8 scan spectra? Does anyone know how the varian spectrometer scales the intensities according to the number of scans? Any suggestion or reply to my query will be extremely useful and greatly appreciated.
Thanks.
Using procheck_nmr on a large number of structures
Linear Mode
