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Figure 5.
Figure 5 Stereo pairs showing refined structures of the
Mg-ADP-bound MJ1267 protein. The molecules are color-coded
according to domain organization (Karpowich et al.,
2001[Karpowich, N., Martsinkevich, O., Millen, L., Yuan, Y.-R.,
Dai, P. L., MacVey, K., Thomas, P. J. & Hunt, J. F. (2001).
Structure, 9, 571-586.]), with green showing the antiparallel
 -sheet
subdomain (ABC ),
red showing the F1-type ATP-binding core, blue showing the  -helical
subdomain (ABC )
and magenta showing the  -phosphate
linker which connects the ABC subdomain
to the ATP-binding core. The images were produced using
MOLSCRIPT and RASTER3D (Kraulis, 1991[Kraulis, P. J. (1991). J.
Appl. Cryst. 24, 946-950.]; Merritt & Bacon, 1997[Merritt, E. A.
& Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]). (a)
Comparison of the structure of one of the NCS-related molecules
in the twinned trigonal crystal (darker colors) with the
structure of the same protein in the untwinned monoclinic
crystal obtained from the methylmercury derivative of the N109C
mutant of MJ1267 (lighter colors) (Karpowich et al.,
2001[Karpowich, N., Martsinkevich, O., Millen, L., Yuan, Y.-R.,
Dai, P. L., MacVey, K., Thomas, P. J. & Hunt, J. F. (2001).
Structure, 9, 571-586.]). The protein has Mg-ADP bound at the
active site in both crystal structures. The molecules were
aligned based on least-squares superposition of the -strands
and P-loop helix from the F1-type ATP-binding core. Subunit A
(the `1+' molecule) is shown from the twinned trigonal crystal
structure. (b) Comparison of the three refined NCS-related
molecules in the asymmetric unit of the twinned trigonal crystal
after least-squares superposition of the the -strands
and P-loop helix from the F1-type ATP-binding core. (c)
Comparison of the three refined NCS-related molecules in the
asymmetric unit of the twinned trigonal crystal after
least-squares superposition of the -helices
in the ABC subdomain.
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