Table I. Data collection and refinement statistics for native and derivative NmrA crystals.
| Data set | Cell dimensions |
Resolution limits (Å) | Reflections |
Completion % | Average I/σI | Rmergea | ||||
|---|---|---|---|---|---|---|---|---|---|---|
| a (Å) | b (Å) | C (Å) | β (°) | Unique | Redundancy | |||||
| Form A native | 76.8 | 76.8 | 104.9 | 20.0–1.8 | 29 825 | 10.6 (8.8) | 88.5 (51.6) | 19.4 (9.2) | 0.065 (0.150) | |
| Form A MMCl | 76.8 | 76.8 | 104.8 | 30.0–2.6 | 11 281 | 8.8 (8.1) | 99.3 (99.2) | 45.6 (17.1) | 0.087 (0.245) | |
| Form A HgCl2 | 76.8 | 76.8 | 104.8 | 30.0–2.3 | 16 314 | 18.8 (15.8) | 98.4 (99.4) | 24.0 (7.2) | 0.087 (0.181) | |
| Form B native | 148.8 | 64.3 | 110.2 | 121.8 | 20.0–1.8 | 78 344 | 5.2 (3.5) | 95.5 (73.3) | 12.8 (1.3) | 0.060 (0.369) |
| Form A NAD | 76.7 | 76.7 | 104.5 | 30.0–1.5 | 54 613 | 8.6 (3.1) | 95.0 (68.4) | 29.5 (2.2) | 0.064 (0.247) | |
| MIRAS analysis 20.0–2.5Å: | R isob | Cullis R factorc |
Phasing powerd |
|||||||
| |
|
|
Centric |
Acentric Iso |
Acentric Anom |
Centric |
Acentric Iso |
Acentric Anom |
||
| MMCl | 0.174 | 0.473 | 0.474 | 0.885 | 2.52 | 3.17 | 1.39 | |||
| HgCl2 | 0.169 | 0.609 | 0.630 | 0.860 | 1.93 | 1.73 | 1.42 | |||
| Mean figure of merit | Centric = 0.51 | Acentric = 0.50 | ||||||||
| Refinement statistics | ||||||||||
| |
Resolution range (Å) |
R factore Rwork/Rfree |
R factore(all data) |
No. of atomsf |
R.m.s. bonds deviation (Å) |
R.m.s. angles deviation (°) |
Mean B factorg |
|
|
|
| Form A | 20.0–1.8 | 0.209/0.258 | 0.205 | 2530/381/4/– | 0.0095 | 1.55 | 22.8/21.5/31.2/– | |||
| Form B | 20.0–1.8 | 0.165/0.202 | 0.164 | 5113/867/7/– | 0.0093 | 1.55 | 27.4/25.5/38.2/– | |||
| Form A NAD | 30.0–1.5 | 0.189/0.222 | 0.182 | 2564/599/7/44 | 0.0091 | 1.54 | 22.0/18.7/35.2/28.9 | |||
Figures in brackets are for outer shell data.
aRmerge = Σ|I – <I>| /Σ<I>
bRiso = Σ|FPH – FP| /ΣFP where FP and FPH are native and derivative structure amplitudes.
cCullis R factor = Σ|||FPH|±ΣFP||–|FH||/Σ||FPH|±|FP||
dPhasing power = <FH>/ε, where ε is the lack of closure error.
eR factor =Σ|Fo – Fc| / ΣFo
fNo. of atoms (protein/water/ions/ligand).
gFor all atoms/protein/water/ligand.