Table 1. Crystallographic data and refinement statistics for crystals of recombinant NC1 chains and their mixtures.
Values in parentheses are for the highest resolution shell.
| α1NC1homo | α2NC1homo | α3NC1homo | α4NC1homo | α5NC1homo | α121NC1 | |
|---|---|---|---|---|---|---|
| Crystallization | ||||||
| Crystallization mixture | 1.4 M Li2SO4, 0.1 M MES pH 6.5 | 22% polyvinylpyrrolidone K15, 0.1 M Na2SO4, 0.1 M MES pH 6.5 | 16% PEG 3350, 0.2 M MgCl2, 0.1 M bis-tris propane pH 7.5 | 6% PEG 3350, 0.2 M Na acetate, 0.1 M MES pH 6.5 | 20% PEG 8000, 0.2 M NaCl, 0.1 M CAPS pH 10.5 | 10% PEG 8000, 0.2 M Mg acetate |
| Additions for crystal harvesting | 15% sucrose, 7.5% ethylene glycol | None | PEG 3350 increased to 40% | Two-step graded increase to 40% PEG 3350 | PEG 8000 increased to 40% | PEG 8000 increased to 20% and 20% sucrose added |
| Data collection | ||||||
| Light source | ID23-2, ESRF | BL13, ALBA | ID23-1, ESRF | ID23-1, ESRF | ID14-1, ESRF | ID29, ESRF |
| Wavelength (Å) | 0.87 | 0.98 | 1.00 | 1.00 | 0.98 | 1.25 |
| Space group | P212121 | I422 | H3 | C2221 | P4132 | P3121 |
| a, b, c (Å) | 94.9, 127.1, 130.5 | 94.3, 94.3, 223 | 131.5, 131.5, 248.9 | 145.6, 167.6, 155.4 | 121.3, 121.3, 121.3 | 126.2, 126.2, 216.2 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 120 | 90, 90, 90 | 90, 90, 90 | 90, 90, 120 |
| Resolution (Å) | 57.12–1.80 (1.90–1.80) | 112.81–2.50 (2.64–2.50) | 65.76–2.70 (2.85–2.70) | 49.44–2.80 (2.95–2.80) | 60.63–1.85 (1.95–1.85) | 48.75–2.82 (2.97–2.82) |
| R merge † (%) | 7.6 (38.8) | 13.4 (168.8) | 8.4 (26.4) | 7.9 (33.6) | 10.0 (35.4) | 9.2 (36.7) |
| R p.i.m. † (%) | 4.8 (24.8) | 2.7 (33.3) | 6.9 (22.3) | 3.2 (13.1) | 4.9 (17.4) | 4.0 (16.6) |
| Mean I/σ(I) | 10.7 (2.8) | 24.1 (2.4) | 11.2 (4.9) | 14.6 (5.6) | 12.1 (4.1) | 12.7 (3.6) |
| Completeness (%) | 98.2 (99.0) | 100 (100) | 98.4 (95.0) | 99.9 (100.0) | 99.3 (99.9) | 98.9 (99.8) |
| Multiplicity | 3.4 (3.3) | 25.2 (26.4) | 2.2 (2.1) | 7.3 (7.5) | 4.8 (4.8) | 5.4 (5.3) |
| Refinement | ||||||
| Resolution (Å) | 57.12–1.80 | 112.81–2.50 | 65.76–2.70 | 49.44–2.80 | 60.63–1.85 | 48.75–2.82 |
| No. of reflections | ||||||
| Total/unique | 479345/142960 | 456608/18124 | 96546/43361 | 341405/46979 | 125648/26393 | 258124/48121 |
| Unique | 68684/20928 | 68350/2593 | 12599/6111 | 51123/6783 | 18482/3812 | 36709/6976 |
| R work/R free (%) | 17.6/19.9 | 24.6/27.9 | 16.3/17.6 | 23.2/28.0 | 18.5/19.0 | 14.1/18.4 |
| Protein chains | 6 | 2 | 8 | 6 | 1 | 6 |
| No. of atoms | ||||||
| Protein | 10612 | 2739 | 13891 | 9603 | 1764 | 10413 |
| Ligands/ions | 52 | 0 | 16 | 0 | 25 | 11 |
| Water | 789 | 55 | 232 | 67 | 116 | 141 |
| B factors (Å2) | ||||||
| Protein | 18.5 | 63.7 | 26.6 | 56.9 | 12.9 | 65.5 |
| Ligands/ions | 24.6 | 0 | 27.1 | 0 | 20.7 | 65.3 |
| Water | 26.7 | 52.9 | 31.2 | 47.6 | 18.8 | 50.9 |
| R.m.s. deviations | ||||||
| Bond lengths (Å) | 0.009 | 0.008 | 0.008 | 0.009 | 0.009 | 0.009 |
| Bond angles (°) | 1.27 | 1.34 | 1.15 | 1.33 | 1.25 | 1.19 |
†
A single crystal was used for each structure.