Table 1. Results of crystallographic studies with 79 mouse homologue proteins that were graded A to D.
| Grade | Proteins* | Crystal hits† (%) | ≥5.0 Å diffraction, no structure‡ (%) | <5.0 Å diffraction, no structure§ (%) | Structures solved¶ (%) |
|---|---|---|---|---|---|
| A | 24 | 16 (67) | 0 (0) | 4 (17) | 4 (17) |
| B | 26 | 22 (85) | 0 (0) | 1 (4) | 9 (35) |
| C | 22 | 18 (82) | 4 (18) | 5 (23) | 2 (9) |
| D | 7 | 6 (86) | 2 (29) | 2 (29) | 0 (0) |
| Total | 79 | 62 | 6 | 12 | 15 |
The classification into four grades, A—D, by 1D 1H NMR screening is described in the text. A and B are proteins that are now routinely forwarded for extensive coarse- and fine-screen crystallization trials, whereas C and D proteins are only subjected to coarse-screen crystallization trials. For details on the 79 proteins, see Table 2.
Number of proteins in each category.
The number of proteins that crystallized in at least one coarse-screen crystallization condition. Two A proteins had been removed from the pipeline for structure determination by NMR.
The number of proteins for which the best crystals diffracted to no higher than 5.0 Å.
The number of proteins for which the best crystals diffracted to better than 5.0 Å, but no structure is as yet available.
The number of proteins for which high-resolution crystal structures have been determined.