Table 2. Summary of Data Collection and Refinement Statistics.
| rBTI-trypsin complex | rBTI | |
| Wavelength (Å) | 1.5418 | 1.00 |
| Space group | P21 | P43212 |
| Resolution rangea (Å) | 12.0−2.26(2.34−2.26) | 15.0−1.84(1.91−1.84) |
| Unique Reflections | 26279 | 8344 |
| Unit Cell (a,b,c) (Å) | 66.7, 50.2, 84.5 | 62.7,62.7,45.9 |
| Completenessa (%) | 99.8(97.7) | 99.8(100) |
| Redundencya | 3.7(3.6) | 24.1(23.2) |
| Averagea b I/σ | 22.6(4.9) | 46.4(4.7) |
| Rmerge a (%) | 5.5(25.3) | 8.0(50) |
| a.s.u content | ||
| No. trypsin | 2 | - |
| No. rBTI | 2 | 1 |
| No. Non-hydrogen atoms | 4247 | 494 |
| No. Ca2+ | 2 | - |
| No. water molecules | 300 | 94 |
| R factor and Rfree (%) | 18.2/22.6 | 19.1/21.6 |
| r.m.s deviations: | ||
| Bond length (Å) | 0.0075 | 0.012 |
| Bond angles (deg) | 1.116 | 1.390 |
| B-factors (Å2): | ||
| Protein | 30.9 | 28.8 |
| Main-chain | 29.5 | 25.7 |
| Side-chain and water | 32.4 | 31.3 |
a
Outer shell values are given in parentheses.
b
I is the intensity; σ is the standard deviation.