3OMU
Crystal Structure of the N-terminal domain of an HSP90 from Trypanosoma Brucei, Tb10.26.1080 in the presence of a thienopyrimidine derivative
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2010-07-14 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 60.044, 60.941, 126.996 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.160 - 2.150 |
| R-factor | 0.2264 |
| Rwork | 0.224 |
| R-free | 0.27300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3o6o |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.236 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 35.000 | 35.000 | 2.190 |
| High resolution limit [Å] | 2.150 | 5.830 | 2.150 |
| Rmerge | 0.071 | 0.031 | 0.724 |
| Number of reflections | 25590 | ||
| <I/σ(I)> | 12.6 | 3.05 | |
| Completeness [%] | 97.8 | 99 | 97.1 |
| Redundancy | 6.7 | 6.2 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 25% PEG 3350 0.2 M Ammonium Acetate 0.1 M Hepes pH 7.5 4 mM MgCl2 2 mM TCEP 2 mM DDU101329, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
