3T29
TMAO-grown trigonal trypsin (bovine)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SEALED TUBE |
| Source details | OXFORD DIFFRACTION NOVA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-05 |
| Detector | OXFORD ONYX CCD |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 54.370, 54.370, 105.355 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.560 - 1.750 |
| R-factor | 0.14791 |
| Rwork | 0.146 |
| R-free | 0.19002 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c1n |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.456 |
| Data reduction software | CrysalisPro |
| Data scaling software | SCALA (3.3.16) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.100 | 19.555 | 1.840 |
| High resolution limit [Å] | 1.750 | 5.530 | 1.750 |
| Rmerge | 0.064 | 0.245 | |
| Number of reflections | 18745 | ||
| <I/σ(I)> | 8.9 | 10.2 | 3.1 |
| Completeness [%] | 99.5 | 97.9 | 97.8 |
| Redundancy | 3.7 | 6.9 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 10 | 298 | 40 mg/mL protein in 50 mM benzamidine, 3 M TMAO, 0.2 M LiNO3, 0.1 M boric acid, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
