 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](hm5067fig2mag.jpg)
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Figure 2
(a) Superimposition of the Cα atoms of the E85I mutant (orange), TFsβ-glucanase (green) and TFsβ-glucanase–CLTR (blue). The structure is orientated so that the reducing end of the sugar (CLTR) is at the top right of the protein molecule, with two eight-β-stranded antiparallel β-sheets. The mean r.m.s.d.s between the E85I mutant and the free enzyme and the enzyme–product complex are 0.7 and 0.9 Å, respectively, for 230 corresponding Cα atoms. Calcium and caesium ions are shown as orange and pink balls, respectively. (b) Ribbon drawing of the overall crystal structure of the E85I mutant structure. Loop A (residues 49–51, cyan) and loop B (residues 72–82, green) located at the bottom of the protein molecule and loop C (residues 142–151, blue) and loop D (residues 203–211, red) located above the protein molecule are indicated. The E85I mutation site is shown in purple and the calcium ion is shown as a gold ball. (c) Left, the crystal-packing interfaces of the E85I mutant molecule and its two symmetry molecules. The residues Gly51 of loop A and Ala78 of loop B of the E85I mutant molecule (x, y, z) are individually associated with residues Ala49 and Asp50 of loop A of the symmetry molecule (y, x, −z). The hydrogen-bonding interactions between loop D residues Ser145 and Gln151 in the symmetry molecule (−x, −x + y, −z + 1/3) and residues Glu16 and Thr133 of the symmetry molecule (y, x, −z) are shown. Right, the monomer in the asymmetric unit is shown in wheat, with two symmetry molecules shown in grey. The loop colours are the same as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) (b). All figures were produced using PyMOL (https://www.pymol.org
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![[Figure 2]](hm5067fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
