TABLE 1.
X-ray data and structure quality statistics for the final refined models of BcCohI
Protein was purified by immobilized metal affinity chromatography followed by gel filtration. Crystals were grown in 0.2 m sodium chloride and 20% w/v PEG 3350 (protein concentration of 15 g/liter). The structure was solved by molecular replacement using PDB code 2ccl as a search model (15). CC½ is the half-data set correlation coefficient. Values in parentheses are for the highest resolution shells.
| Data quality | |
|---|---|
| X-ray source | ESRF, beamline ID14-4 |
| Wavelength (Å) | 0.9393 |
| Unit cell parameters | a = 30.38 Å |
| b = 52.77 Å | |
| c = 90.46 Å | |
| Space group | P212121 |
| Resolution of data (Å) | 42.93-1.84 |
| Total reflections | 93,268 (3119) |
| Unique reflections | 13,158 (1293) |
| Multiplicity | 7.0 (3.8) |
| Completeness (%) | 99.46 (98.40) |
| Mean I/σ(I) | 8.9 (1.3) |
| Wilson B-factor | 23.64 |
| Rmergea | 0.161 (1.014) |
| Rpimb | 0.057 (0.567) |
| CC1/2 | 0.995 (0.549) |
| Mosaicity | 0.34 |
| Rwork | 0.1842 (0.2962) |
| Rfree | 0.2566 (0.3301) |
| No. of non-hydrogen atoms | 1389 |
| Macromolecules | 1222 |
| Water | 167 |
| Protein residues | 154 |
| Root mean square (bonds) | 0.015 |
| Root mean square (angles) | 1.76 |
| Ramachandran favored (%) | 93 |
| Ramachandran outliers (%) | 0 |
| Clash score | 8.21 |
| Average B-factor | 31.1 |
| Macromolecules | 29.9 |
| Solvent | 40 |
| PDB code | 4ums |
a Rmerge = Σh Σi|I(h,i) − 〈I(j)〉|/Σh Σi I(h,i), where I(h,i) is the intensity of the measurement of reflection h and 〈I(h)〉 is the mean value of I(h,i) for all i measurements.
b Rpim= (Σhkl√1/(n − 1)Σj = 1n|Ihkl,j − 〈Ihkl〉|)/Σhkl Σj Ihkl,j), where 〈Ihkl〉 is the average of symmetry-related observations of a unique reflection.