Table 1. Crystallographic data for the CypD structures.
Values in parentheses are for the highest resolution shell.
| CypD-t | CypD-o | |
|---|---|---|
| Data collection | ||
| Unit-cell parameters (Å) | a = b = 57.02, c = 87.16 | a = 40.56, b = 57.01, c = 57.34 |
| Space group | P41212 | P212121 |
| Resolution (Å) | 47.72–0.85 (0.86–0.85) | 40.56–1.45 (1.47–1.45) |
| Wavelength (Å) | 1.0000 | 1.0000 |
| Temperature (°C) | −173 | −173 |
| Observed reflections | 1755792 | 155848 |
| Unique reflections | 123449 | 24241 |
| 〈I/σ(I)〉 | 30.7 (1.8) | 12.4 (1.8) |
| Completeness (%) | 97.7 (60.2) | 99.9 (100) |
| Multiplicity | 14.2 (1.7) | 6.4 (6.5) |
| R merge † (%) | 4.9 (34.2) | 9.7 (112.0) |
| R meas ‡ (%) | 5.0 (45.3) | 10.6 (121.8) |
| R p.i.m. ‡ (%) | 1.1 (29.4) | 4.2 (47.1) |
| CC1/2 § | 0.999 (0.766) | 0.999 (0.715) |
| Refinement | ||
| Resolution (Å) | 28.51–0.85 (0.86–0.85) | 33.12–1.45 (1.51–1.45) |
| Reflections (working/test) | 117150/6189 (1964/108) | 22858/1231 (2421/142) |
| R factor/R free ¶ (%) | 10.7/11.9 (26.8/30.2) | 16.0/19.0 (23.8/27.9) |
| No. of atoms | ||
| Protein | 1266 | 1237 |
| PEG 400 | 16 | 10 |
| Water | 303 | 133 |
| Model quality | ||
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.015 | 0.008 |
| Bond angles (°) | 1.482 | 0.909 |
| Average B factor (Å2) | ||
| All atoms | 8.1 | 19.0 |
| Protein | 5.7 | 17.8 |
| PEG 400 | 11.1 | 34.6 |
| Water | 17.5 | 29.5 |
| Coordinate error (maximum likelihood) (Å) | 0.05 | 0.19 |
| Ramachandran plot | ||
| Most favored (%) | 97.0 | 96.4 |
| Additionally allowed (%) | 3.0 | 3.6 |
†
R
merge = 
, where Ii(hkl) is the intensity measured for the ith reflection and 〈I(hkl)〉 is the average intensity of all reflections with indices hkl.
‡
R meas is the redundancy-independent (multiplicity-weighted) R merge (Evans, 2006 ▶, 2011 ▶). R p.i.m. is the precision-indicating (multiplicity-weighted) R merge (Diederichs & Karplus, 1997 ▶; Weiss, 2001 ▶).
§
CC1/2 is the correlation coefficient of the mean intensities between two random half-sets of data (Karplus & Diederichs, 2012 ▶; Evans, 2012 ▶).
¶
R factor = 
; R
free is calculated in an identical manner using 5% of randomly selected reflections that were not included in the refinement.