Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 Å resolution

Murayama, K.; Kato-Murayama, M.; Katsura, K.; Uchikubo-Kamo, T.; Yamaguchi-Hirafuji, M.; Kawazoe, M.; Akasaka, R.; Hanawa-Suetsugu, K.; Hori-Takemoto, C.; Terada, T.; Shirouzu, M.; Yokoyama, S.

doi:10.1107/S1744309104032555

Acta Crystallographica Section F
Acta Crystallographica
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Figure 1
(a) Quality of the electron-density map. The refined structure is represented by a thin wire. The map is contoured at the 1.0σ level. (b) Stereo diagram of the APE2540 protein. The secondary structures are coloured blue (α-helices) and red (β-strands). (c) Comparison of the structural homologues of the APE2540 protein. The three structures are coloured and oriented in the same direction as in Fig. 1

(b). Figs. 1(b) and 1(c) were produced with Molscript (Kraulis, 1991

) and Raster3D (Merritt & Bacon, 1997

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 61| Part 1| December 2005| Pages 26-29

doi:10.1107/S1744309104032555

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