1A28
HORMONE-BOUND HUMAN PROGESTERONE RECEPTOR LIGAND-BINDING DOMAIN
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-09-12 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 58.123, 64.444, 69.954 |
Unit cell angles | 90.00, 95.74, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.800 |
R-factor | 0.1905 |
Rwork | 0.191 |
R-free | 0.22790 * |
Structure solution method | MAD, MIR |
RMSD bond length | 0.008 |
RMSD bond angle | 1.393 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | DPHASE |
Refinement software | CNS (0.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.055 | 0.055 |
Number of reflections | 42976 | |
<I/σ(I)> | 18.3 | 3.4 |
Completeness [%] | 93.2 | 95.9 |
Redundancy | 3.2 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 * | 4 * | PROTEIN WAS CRYSTALLIZED FROM 2% PEG 4000, 50 MM PIPES PH 6.5, 350 MM LI2SO4, THEN STABILIZED IN THE SAME BUFFER WITH 21% ETHYLENE GLYCOL |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | HEPES | 6.7 (mM) | |
10 | 1 | drop | PEG4000 | 0.7 (%) | |
11 | 1 | reservoir | PIPES | 50 (mM) | |
12 | 1 | reservoir | 350 (mM) | ||
13 | 1 | reservoir | PEG4000 | 2 (%) | |
14 | 1 | reservoir | glycerol | 10 (%) | |
2 | 1 | drop | glycerol | 10 (%) | |
3 | 1 | drop | dithiothreitol | 3.3 (mM) | |
4 | 1 | drop | beta-octylglucoside | 0.06 (%) | |
5 | 1 | drop | progesterone | 6.7 (nM) | |
6 | 1 | drop | 93 (mM) | ||
7 | 1 | drop | protein | 4 (mg/ml) | |
8 | 1 | drop | PIPES | 17 (mM) | |
9 | 1 | drop | 117 (mM) |