3PEH
Crystal Structure of the N-terminal domain of an HSP90 from Plasmodium Falciparum, PFL1070c in the presence of a thienopyrimidine derivative
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-08-18 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | .97926 |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 91.927, 91.927, 162.884 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.330 - 2.750 |
| R-factor | 0.2237 |
| Rwork | 0.222 |
| R-free | 0.26330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1zw9 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.150 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.8.0) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 35.000 | 35.000 | 2.800 |
| High resolution limit [Å] | 2.750 | 7.440 | 2.750 |
| Rmerge | 0.097 | 0.041 | 0.939 |
| Number of reflections | 18792 | ||
| <I/σ(I)> | 10.2 | 2.95 | |
| Completeness [%] | 99.9 | 99.3 | 100 |
| Redundancy | 9.5 | 8 | 9.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 30 % PEG 5k MME 0.2 M Ammonium sulfate 0.1 M MES pH 6.5 1 mM DDU compound 4 mM MgCl2 2 mM TCEP glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
