Practical considerations over spectral quality in solid state NMR spectroscopy of
soluble proteins
Marco Fragai, Claudio Luchinat, Giacomo Parigi and Enrico Ravera
Contribution from Center for Magnetic Resonance (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto
Fiorentino (FI), Italy and Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto
Fiorentino (FI), Italy
Corresponding Author:
Prof. Claudio Luchinat
CERM, University of Florence
Via Sacconi 6, 50019 Sesto Fiorentino, Italy
Tel +39 055 4574296
FAX +39 055 4574253
Email: claudioluchinat@cerm.unifi.it
Supplementary materials
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Table S1. Limiting concentrations observed for some biomolecular sediments, compared to
the corresponding crystals, reported as volume fraction. Volume fraction in crystals is
obtained from the x-ray structures, volume fraction in sediments is calculated from the
observed limiting concentrations (mg/ml) and the protein density obtained from the
molecular weight and the protein volume calculated with the algorithm described in (Voss
and Gerstein, 2005) and implemented in helixweb.nih.gov/structbio/basic.html.
Protein
Volume
Volume fraction
fraction in
in sediments
References
crystals
Albumin (4F5S)
0.51
0.52
(Lundh, 1980;
Bujacz, 2012)
Chymotrypsinogen
0.36
0.51
(Lundh, 1980;
(1EX3)
DNAb Helicase
Pjura et al., 2000)
0.29
0.15
(Gardiennet et al.,
2012)
Ferritin (1MFR)
0.29
0.5
(Bertini et al.,
2012; Ha et al.,
1999)
Lysozyme (2VB1)
0.73
0.47-0.56
(Gregory et al.,
1993; Wang et al.,
2007)
2
Methemoglobin
0.54
0.62
(Lundh, 1985;
(1Y8H)
Sankararayanan et
al., 2005)
Transferrin (3QYT)
0.49
0.5
(Lundh, 1980;
Lundh, 1985; Yang
et al., 2012)
Ubiquitin (3ONS)
0.48
0.54
Present study,
(Huang et al., 2011)
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Reference List
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68:1278-1289
Gardiennet C, Schütz AK, Hunkeler A, Kunert B, Terradot L, Böckmann A and Meier BH (2012)
A Sedimented Sample of a 59 kDa Dodecameric Helicase Yields High-Resolution SolidState NMR Spectra. Angew Chem Int Ed 51:7855-7858
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Lundh S (1985) Ultacentrifugation of concentrated biopolymer solutions and effect of
ascorbate. Archives of Biochemistry and Biophysics 241:265-274
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Sankararayanan R, Biswal BK and Vijayan M (2005) A new relaxed state in horse
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comparison with proteins: RNA is packed more tightly. J Mol Biol 346:477-492
Wang J, Dauter M, Alkire R, Joachimiak A and Dauter Z (2007) Triclinic lysozyme at 0.65 A
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transferrin reveals a partially-opened conformation in the N-lobe. Sci Rep 2:999
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