1AH8
STRUCTURE OF THE ORTHORHOMBIC FORM OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.5 |
Synchrotron site | SRS |
Beamline | PX9.5 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-09 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 115.540, 112.900, 44.720 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.100 |
R-factor | 0.196 |
Rwork | 0.196 |
R-free | 0.25500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | TETRAGONAL FORM |
RMSD bond length | 0.006 |
RMSD bond angle | 26.100 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | TFFC |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.150 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.033 | 0.033 |
Number of reflections | 34954 | |
<I/σ(I)> | 12.8 | 7.9 |
Completeness [%] | 99.7 | 92.6 |
Redundancy | 3.5 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.4 * | Prodromou, C., (1996) Proteins: Struct.,Funct., Genet., 25, 517. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 36 (mg/ml) | |
2 | 1 | 1 | PEGME550 | 3 (%) | |
3 | 1 | 1 | 20 (mM) | ||
4 | 1 | 1 | Tris | 10 (mM) |