Table 2.

Statistics of data collection and refinement.

Complex	E. coli: GDP•2′-deoxy-6-PIMP•hadacidin	Mouse muscle: GDP•2′-deoxy-6-PIMP
Space group	P3221	P43212
Unit cell parameters:
a (Å)	80.59	70.11
b (Å)	80.59	70.11
c (Å)	158.5	199.0
Resolution limits (Å)	25–2.0	16–2.4
No. of reflections collected	285,758	244,020
No. of unique reflections	39,551	20,371
Completeness of data (%), overall/last shella	96.4/78.5	98.9/98.9
Rmergeb, overall/last shella	0.055/0.265	0.100/0.415
No. of refls. In refinementc	39,498	19,121
No. of atoms	3,384	3,408
No. of solvent sites	169	128
R/Rfreed	0.224/0.251	0.198/0.262
Mean B values (Å2):
Protein	38	35
Ligands	36	27
Root mean square deviations:
Bond lengths(Å)	0.006	0.006
Bond angles(°)	1.3	1.2
Dihedral angles(°)	23	23
Improper dihedral angles(°)	0.83	0.85

^aResolution range for the last shell is 2.0–2.07 Å for the E. coli complex and 2.4–2.5 Å for mouse muscle complex.

^bR_merge=Σ_jΣ_i|I_ij−<I_j>|/Σ_iΣ_jI_ij, where i runs over multiple observations of the same intensity and j runs over crystallographically unique intensities.

^cAll data for which |F_obs|>0.

^dR-factor=Σ||F_obs|−|F_calc||/Σ|F_obs|, |F_obs|>0.