 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](pg5072fig2mag.jpg)
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Figure 2
(a) The 1H–15N HSQC spectrum of 13C- and 15N-labeled reduced Ec-Trx (∼1.0 mM) collected at a proton resonance frequency of 750 MHz at 20°C in 100 mM NaCl, 20 mM Tris, 1 mM DTT pH 7.0, with the assigned amide cross peaks labeled. Gly84 (underlined) is folded into the spectrum and Gly6, at 9.20 (1H) and 107.4 (15N) p.p.m., is not shown. (b) The 1H–15N HSQC spectrum of 13C- and 15N-labeled oxidized Ec-Trx (∼1.0 mM) collected at a proton resonance frequency of 600 MHz at 20°C in 100 mM NaCl, 20 mM Tris pH 7.0, with the assigned amide cross peaks labeled. Not shown is the cross peak for Gly84 at 9.85 (1H) and 103.9 (15N) p.p.m. In both spectra the backbone amide cross peaks from the non-native N-terminal tag are identified with red labels, cross peaks below the displayed contour levels are identified with an `x', side-chain amide resonance cross-peak pairs are connected by a red dashed line and the eight amide cross peaks that are absent in Fig. 2 ![[link]](../../../../../../logos/arrows/f_arr.gif) (a) are circled in orange in Fig. 2(b). |
![[Figure 2]](pg5072fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
