Table 2. Summarized data collection and structure refinement statistics.
| Diffraction resolution, Å | 1.9 |
| Space group | P212121 |
| Unit cell, Å | a = 69.56, b = 74.69, c = 103.69 |
| Final R-factor* (Rfree), % | 20.2 (22.4) |
| No. of residues† | |
| Protein | 494 (14) |
| Waters | 284 |
| Maltose | 1 |
| rmsd angles, ° | 1.1 |
| rmsd bonds, Å | 0.0049 |
Complete data statistics are available in Table 5, which is published as supporting information on the PNAS web site. rmsd, rms deviation.
*
R-factor = Σhkl∥Fobs| — |Fcalc∥/Σhkl| Fobs|. Rfree is computed in the same manner as the R-factor with the test set of reflections (5%).
†
The values in parentheses are for number of missing residues.