Table 1. Crystallographic Data and Refinement Statistics.
| Data collection | ||
| Data sets | LGN/mInsc | LGN/NuMA |
| Space group | C2 | P6122 |
| Unit cell (Å) | a=88.196, b=75.606, c=35.346 |
a=91.305, b=91.305, c=178.376 |
| Resolution range (Å) | 50.00-1.10 (1.12-1.10) | 50.00-2.30 (2.34-2.30) |
| No. of unique reflections | 84934 (2703) | 20308 (984) |
| Rmerge (%) | 4.8 (51.1) | 8.7 (65.6) |
| I/s | 29.7(2.4) | 35.5 (4.9) |
| Redundancy | 5.3 (3.2) | 17.6 (16.6) |
| Completeness (%) | 94.4 (60.6) | 99.7 (99.9) |
|
| ||
| Refinement | ||
| Resolution (Å) | 20.00-1.10 (1.16-1.10) | 36.1-2.30 (2.36-2.30) |
| Rcryst/Rfree (%) | 12.0 (21.1)/15.0 | 21.5(22.9)/27.1(30.3) |
| No. of atoms | ||
| Proteins | 1536 | 2671 |
| Water | 316 | 103 |
| Other atoms | 14 | 18 |
| No. of reflections | ||
| Working set | 80648 | 18723 |
| Test set | 4259 | 1585 |
| Mean B factor of protein/peptide | ||
| Main chain | 11.0/14.5 | 49.8/90.4 |
| Side chain | 15.1/22.9 | 51.8/93.7 |
| R.m.s. deviations | ||
| Bond length (Å) | 0.014 | 0.008 |
| Bond angles (°) | 0.030 | 1.00 |
| Ramachandran plot (%) | ||
| Most favored | 98.63 | 97.08 |
| Additionally allowed | 1.37 | 2.34 |
| generously allowed | 0 | 0.58 |
1
Numbers in parentheses represent the value for the highest resolution shell.
2
Rmerge = SUM (ABS(I - <I>)) / SUM (I), where I is the intensity of measured reflection and <I> is the mean intensity of all symmetry-related reflections.
3
Rcryst= Σ|Fcalc − Fobs|/ΣFobs,where Fobs and Fcalc are observed and calculated structure factors.
4
Rfree= ΣT|Fcalc − Fobs|/ΣFobs, where T is a test data set of about 5% of the total unique reflections randomly chosen and set aside prior to refinement.
5
B factors are caculated by combining the residual B-factor and TLS parameters using TLSANL program in CCP4.