1PV2
Native Form 2 E.coli Chaperone Hsp31
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-01-13 |
Wavelength(s) | 1.77 |
Spacegroup name | P 1 |
Unit cell lengths | 54.487, 99.018, 116.795 |
Unit cell angles | 102.95, 101.52, 94.19 |
Refinement procedure
Resolution | 20.000 * - 2.700* |
R-factor | 0.22469 |
Rwork | 0.221 |
R-free | 0.28700 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1n57 |
RMSD bond length | 0.004 |
RMSD bond angle | 0.793 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.800 | 2.800 |
High resolution limit [Å] | 2.700 * | 2.700 |
Rmerge | 0.075 | 0.339 |
Number of reflections | 60105 * | |
<I/σ(I)> | 9.4 | 2 |
Completeness [%] | 96.1 * | 94.1 * |
Redundancy | 1.9 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.4 * | 295 | 26% PEG 6000,50mM NaCl,100 mM Tris pH 7.5.5G, VAPOR DIFFUSION, SITTING DROP, temperature 22K, temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 2 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 50 (mM) | pH7.4 |
3 | 1 | drop | 100 (mM) | ||
4 | 1 | drop | EDTA | 1 (mM) | |
5 | 1 | drop | dithiothreitol | 4 (mM) | |
6 | 1 | reservoir | PEG6000 | 26 (%) | |
7 | 1 | reservoir | 50 (mM) | ||
8 | 1 | reservoir | Tris | 100 (mM) | pH7.5 |