Table 1.

Model Refinement and Validation Statistics^a

	Amikacin-Ribosome 50S	Amikacin-Ribosome 30S Body	Amikacin-Ribosome 30S Head	Tigecycline-Ribosome 50S	Tigecycline-Ribosome 30S Body	Tigecycline-Ribosome 30S Head
Map resolution (Å) (FSC = 0.143)	2.7	2.9	3.0	2.5	2.7	3.0
Map sharpening B factor (Å2)	−47.3	−55.7	−51.6	−82.5	−99.3	−131.4
Model Composition
Non-hydrogen atoms	83,514	33,322	16,864	83,855	33,279	16,906
Protein residues	3,069	1,496	852	3,112	1,496	852
Nucleic acid residues	2,800	1,040	477	2,800	1,040	477
Metal ions	161	59	24	163	56	24
Ligand	none	amikacin	none	tigecycline ×3	none	tigecycline
General Validation
CCb (model to map fit)	0.86	0.83	0.86	0.86	0.84	0.70
Clashscore	4.84	7.09	5.25	5.86	9.42	15.11
Root-mean-square Deviations
Bond lengths (Å)	0.007	0.012	0.007	0.008	0.010	0.007
Bond angles (°)	0.775	0.974	0.702	0.730	0.794	0.853
Protein Geometry Validation
Rotamer outliers (%)	7.08	11.02	7.15	5.70	8.22	11.24
Ramachandran outliers (%)	0.03	0.20	0.00	0.07	0.00	0.24
Ramachandran favored (%)	94.46	90.54	92.58	95.42	91.90	91.03
RNA Geometry Validationc
Sugar pucker outliers (%)	0.64	0.38	0.21	0.57	0.38	0.42
Backbone conformation outliers (%)	17.14	20.48	17.19	15.89	19.71	22.85

^aObtained from Phenix refinement log unless otherwise stated.

^bCC, correlation coefficient.

^cObtained from MolProbity Web server.