Table 1 Statistics of data collection and structure refinement
From: Protecting role of cosolvents in protein denaturation by SDS: a structural study
Form I | Form II | |
|---|---|---|
Expected MPD concentration in the drop after equilibration | close to 0 M | >4 M |
Expected SDS concentration in the protein droplet | ~2 mM | ~5 mM |
Data collection | ||
Space group | P43212 | P43212 |
Unit-cell parameters (Ǻ) | a = b = 77.59, c = 37.57 | a = b = 77.90, c = 37.53 |
Maximum resolution (Ǻ) | 2.3 | 1.75 |
Unique reflections | 5468 | 12247 |
Redundancy | 8.1 | 10.1 |
Completeness (%) | 99.7(100) | 99.7(99.9) |
Avg. I/σ | 21.9(8.5) | 18.7(3.2) |
R merge (%) | 8.22(22.72) | 4.5(20.2) |
Refinement statistics | ||
R (%) a | 20.18 | 17.03 |
R free (%) a | 21.40 | 20.84 |
RMSD bond lengths (Ǻ) | 0.021 | 0.066 |
RMSD angle distances (Ǻ) RMSD bond angles (°) | 1.92 | 0.061 |
Average B value (Ǻ 2 ) | ||
Protein atoms | 14.91 | 14.63 |
MPD molecules | / | 53.47 |
SDS molecule | 45.94 | / |
Water molecules | 20.66 | 26.64 |
Ramachandran plot Most favored, additional, generously allowed (%) | 85.0/13.3/1.8 | 89.4/10.6/0.0 |
No. of MPD molecules | 0 | 2 |
No. of SDS molecules | 1 | 0 |
No. of Na ion | 0 | 1 |
No. of Cl ion | 0 | 2 |
No. of water molecules | 69 | 118 |