1IXG
PHOSPHATE-BINDING PROTEIN MUTANT WITH THR 141 REPLACED BY ASP (T141D), COMPLEXED WITH PHOSPATE
Experimental procedure
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-07 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.645, 63.493, 123.788 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.100 - 1.050 |
R-factor | 0.109 |
R-free | 0.13900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pbp |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXL-96 |
Refinement software | SHELXL-96 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.100 | 1.090 |
High resolution limit [Å] | 1.050 | 1.050 |
Rmerge | 0.048 | 0.157 |
Number of reflections | 111988 | |
<I/σ(I)> | 29.5 | 3.8 |
Completeness [%] | 71.7 | 32.2 |
Redundancy | 7.7 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.5 | Wang, Z., (1994) J.Biol.Chem., 269, 25091. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7.25 (mg/ml) | |
2 | 1 | drop | potassium phosphate | 1.5 (mM) | |
3 | 1 | drop | PEG6000 | 13.5 (%(w/v)) | |
4 | 1 | drop | 37.5 (mM) | ||
5 | 1 | drop | potassium acetate | 15 (mM) | |
6 | 1 | reservoir | PEG6000 | 18 (%(w/v)) | |
7 | 1 | reservoir | 50 (mM) | ||
8 | 1 | reservoir | potassium phosphate | 2 (mM) | |
9 | 1 | reservoir | potassium acetate | 20 (mM) |