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Results: 4

1.
Scheme 1

Scheme 1. From: Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods.

(a) Amino acid sequence of plectasin.1 (b) Synthetic strategy used for the total chemical synthesis of plectasin by native chemical ligation. R = -CH2CH2CO-Ala-COOH.

Kalyaneswar Mandal, et al. Protein Sci. 2009 June;18(6):1146-1154.
2.
Figure 2

Figure 2. From: Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods.

X-ray structure of l-plectasin determined by racemic crystallography. (a) Ribbon representation of l-plectasin; the ribbon is colored by B-factor values. (b) Superposition of the NMR structure (PDB ID: 1zfu) of plectasin (in red) and the present X-ray crystal structure (in blue). The Cα-traces are shown. The disulfide bridges are included as sticks with larger radius; the coloring scheme matches the Cα-traces. The selected NMR model (#4) displays the minimal r.m.s. deviation of 1.1 Å. (c) SigmaA-weighted 2Fo-Fc electron density map of plectasin crystallized in space group, contoured at 2σ encompassing three disulfide bridges. (b, c) were made with Pymol21 and (a) was prepared with Ribbons.22

Kalyaneswar Mandal, et al. Protein Sci. 2009 June;18(6):1146-1154.
3.
Figure 3

Figure 3. From: Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods.

Crystal packing. (a) Centrosymmetric unit cell. The l-plectasin molecule is shown in blue and the d-plectasin molecule is in gold. (b) Close-up view of the packing interface [boxed in panel (a)] between the l- and d-enantiomers forming the unit cell. (c) Chiral P61 unit cell. Six neighboring l-plectasin molecules are shown in blue and cyan. (d) The packing interface (boxed in panel c) between the two closest l-plectasin molecules in P61 space group. In panels (b) and (d) water molecules are shown as small magenta spheres and hydrogen bonds are shown as dashed lines. The figures were prepared in Ribbons. The hydrogen bond distances are listed in Supporting Information Tables S3 and S4 for and P61 space groups, respectively.

Kalyaneswar Mandal, et al. Protein Sci. 2009 June;18(6):1146-1154.
4.
Figure 1

Figure 1. From: Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods.

The LC-MS profiles of the purified synthetic plectasin enantiomers. (a) l-plectasin (obs. = 4401.2 ± 0.5 Da, calc. = 4400.8 Da (high point of isotope distribution) (b) d-plectasin (obs. = 4401.2 ± 0.5 Da, calc. = 4400.8 Da (high point of isotope distribution). The chromatographic separations were performed using a linear gradient (5%–65%) of buffer B in buffer A over 15 min (buffer A = 0.1% trifluoroacetic acid (TFA) in water; buffer B = 0.08% TFA in acetonitrile) on an in-house packed 3 μm C-4, 2.1 × 50 mm column at 40°C with detection at 214 nm and on-line ion trap electrospray MS.

Kalyaneswar Mandal, et al. Protein Sci. 2009 June;18(6):1146-1154.

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