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. Author manuscript; available in PMC: 2011 Oct 13.
Published in final edited form as: J Am Chem Soc. 2010 Oct 13;132(40):14229–14238. doi: 10.1021/ja106175q

Table 3.

Crystallographic data collection and refinement statistics

Data set1 nNOS-3a nNOS-3b nNOS-3c nNOS-3d
Data collection
PDB code 3NLV 3NLX 3NLY 3NLZ
Space group P212121 P212121 P212121 P212121
Cell dimensions
 a, b, c (Å) 52.3, 111.7, 164.4 52.3, 111.5, 164.4 51.8, 111.2, 164.1 51.9, 110.4, 164.0
Resolution (Å) 2.10 (2.14-2.10) 1.87 (1.90-1.87) 2.00 (2.03-2.00) 1.92 (1.95-1.92)
Rsym or Rmerge 0.080 (0.59) 0.053 (0.36) 0.078 (0.40) 0.050 (0.32)
I/σI 9.1 (2.2) 13.5 (3.9) 7.6 (1.8) 11.5 (2.6)
No. unique reflections 56,857 79,054 63,439 73,017
Completeness (%) 99.4 (99.5) 98.2 (96.5) 96.7 (80.9) 99.4 (89.8)
Redundancy 5.6 (2.9) 4.1 (4.1) 3.9 (3.1) 4.1 (3.6)
Refinement
Resolution (Å) 2.10 1.87 2.00 1.92
No. reflections used 54,011 75,069 60,245 69,320
Rwork/Rfree 0.175/0.211 0.178/0.209 0.201/0.249 0.173/0.210
No. atoms
 Protein 6,671 6,689 6,676 6,707
 Ligand/ion 187 223 190 217
 Water 434 479 190 417
R.m.s. deviations
 Bond lengths (Å) 0.013 0.012 0.015 0.013
 Bond angles (°) 1.325 1.390 1.554 1.456
Data set1 nNOS-3e nNOS-3f eNOS-3b eNOS-3f
Data collection
PDB code 3NM0 3NLW 3NLU 3NLT
Space group P212121 P212121 P212121 P212121
Cell dimensions
 a, b, c (Å) 52.1, 110.9, 164.2 52.2, 111.4, 164.7 58.0, 107.0, 156.9 57.9, 106.9, 157.0
Resolution (Å) 1.81 (1.84-1.81) 2.10 (2.14-2.10) 2.65 (2.70-2.65) 2.75 (2.80-2.75)
Rsym or Rmerge 0.048 (0.38) 0.069 (0.55) 0.121(0.58) 0.103 (0.65)
I/σI 12.1 (2.7) 9.2 (2.4) 9.7 (1.9) 12.4 (1.9)
No. unique reflections 86,908 56,364 28,366 25,670
Completeness (%) 99.0 (92.5) 99.2 (100.0) 97.3 (99.1) 95.6 (94.4)
Redundancy 4.0 (3.8) 4.1 (4.1) 3.7 (3.7) 3.9 (4.0)
Refinement
Resolution (Å) 1.81 2.10 2.65 2.74
No. reflections used 82,532 53,523 26,957 24,379
Rwork/Rfree2 0.178/0.209 0.171/0.207 0.185/0.254 0.186/0.262
No. atoms
 Protein 6,716 6,676 6,451 6,419
 Ligand/ion 217 185 197 195
 Water 459 319 111 60
R.m.s. deviations
 Bond lengths (Å) 0.013 0.013 0.014 0.014
 Bond angles (°) 1.360 1.347 1.502 1.519
1

See Schemes 2, 3, and 4 for nomenclature and chemical formula of inhibitors.

2

Rfree was calculated with the 5% of reflections set aside throughout the refinement. For each NOS isoform the set of reflections for the Rfree calculation were kept the same for all data sets according to those used in the data of the starting model.