1AE9
STRUCTURE OF THE LAMBDA INTEGRASE CATALYTIC CORE
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 113 |
Detector technology | IMAGE PLATE |
Collection date | 1996-02-10 |
Detector | MARRESEARCH |
Spacegroup name | H 3 |
Unit cell lengths | 107.320, 107.320, 108.710 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 16.000 - 1.900 |
R-factor | 0.199 |
Rwork | 0.199 |
R-free | 0.23200 |
Structure solution method | MIRAS |
RMSD bond length | 0.007 |
RMSD bond angle | 1.131 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.851) |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 16.000 | 1.930 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.042 * | |
Total number of observations | 110468 * | |
Number of reflections | 36385 * | |
<I/σ(I)> | 12.9 | 4 |
Completeness [%] | 98.9 | 99.5 |
Redundancy | 2.8 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.15 | 22 * | PROTEIN WAS CRYSTALLIZED FROM 20% PEG 8000 75 MM NACL 7 MM MGCL2 50 MM MES, PH 6.15 40 MM NACITRATE 1 MM DTT 1 MM SPERMINE |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | c170 | 26 (mg/ml) | |
2 | 1 | reservoir | MES | 50 (mM) | |
3 | 1 | reservoir | 75 (mM) | ||
4 | 1 | reservoir | 7 (mM) | ||
5 | 1 | reservoir | sodium citrate | 40 (mM) | |
6 | 1 | reservoir | DTT | 1 (mM) | |
7 | 1 | reservoir | EDTA | 0.1 (mM) | |
8 | 1 | reservoir | spermine-HCl | 1 (mM) |