One of our diffractometers is equipped with a Incoatec Microsource (ImuS) x-ray tube emmitting copper radiation. Although the tube runs on low power, the flux density it emmits beats that of most standard roatating anodes. This instrument allows us to collect diffraction data from protein crystals with a data quality comparable to or better than what can be obtained with typical protein in-house diffractometers.
The table below gives the data statistics for a tetragonal HEW-lysozyme crystal, which is one of the most common test crystals used for protein diffraction. The data collection took only 22 hours and for scientists familiar with lysozyme it is obvious that the instrument that collected these data does not need to hide.
Resolution | Completeness | Redundancy | I/sigma | Rmerge | Rsigma |
---|---|---|---|---|---|
Inf – 5.16 | 99.5 | 9.82 | 57.62 | 0.0305 | 0.0162 |
5.16 – 3.36 | 99.8 | 9.89 | 52.33 | 0.0245 | 0.0176 |
3.36 – 2.63 | 99.9 | 10.55 | 49.58 | 0.0353 | 0.0174 |
2.63 – 2.29 | 100.0 | 17.54 | 56.46 | 0.0449 | 0.0149 |
2.29 – 2.07 | 100.0 | 18.18 | 49.44 | 0.0580 | 0.0166 |
2.07 – 1.92 | 100.0 | 15.11 | 36.63 | 0.0717 | 0.0224 |
1.92 – 1.80 | 100.0 | 13.92 | 27.50 | 0.0874 | 0.0306 |
1.80 – 1.71 | 100.0 | 13.31 | 21.68 | 0.1058 | 0.0405 |
1.71 – 1.63 | 100.0 | 12.72 | 17.45 | 0.1283 | 0.0511 |
1.63 – 1.57 | 100.0 | 12.21 | 14.94 | 0.1524 | 0.0611 |
1.57 – 1.51 | 100.0 | 11.71 | 11.30 | 0.2027 | 0.0820 |
1.51 – 1.46 | 100.0 | 11.30 | 9.37 | 0.2326 | 0.0988 |
1.46 – 1.42 | 100.0 | 10.89 | 7.75 | 0.2703 | 0.1230 |
1.42 – 1.38 | 100.0 | 10.55 | 6.26 | 0.3142 | 0.1531 |
1.38 – 1.35 | 100.0 | 10.18 | 5.05 | 0.3790 | 0.1923 |
1.35 – 1.31 | 100.0 | 9.83 | 4.48 | 0.4069 | 0.2151 |
1.31 – 1.29 | 99.3 | 7.60 | 3.56 | 0.4318 | 0.2743 |
1.29 – 1.26 | 96.2 | 5.03 | 2.85 | 0.4136 | 0.3594 |
1.26 – 1.23 | 95.9 | 4.86 | 2.44 | 0.4612 | 0.4186 |
1.23 – 1.21 | 91.5 | 3.89 | 2.00 | 0.5012 | 0.5061 |
1.21 – 1.18 | 66.6 | 1.40 | 1.39 | 0.5012 | 0.7304 |
Inf – 1.22 | 99.3 | 11.08 | 20.52 | 0.0640 | 0.0308 |