1O4S
Crystal structure of Aspartate aminotransferase (TM1255) from Thermotoga maritima at 1.90 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-04-16 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.048, 79.509, 170.184 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.000 - 1.900 |
R-factor | 0.16 |
Rwork | 0.159 |
R-free | 0.20000 |
Structure solution method | MR |
Starting model (for MR) | 1bkg |
RMSD bond length | 0.017 |
RMSD bond angle | 1.620 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA (4.2)) |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.000 * | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.063 * | 0.422 * |
Total number of observations | 249027 * | |
Number of reflections | 59510 | |
<I/σ(I)> | 15.9 | 1.7 |
Completeness [%] | 85.8 | 50.6 |
Redundancy | 4.8 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.9 * | 293 | 2.4 (NH4)2SO4 9 CHES , VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Tris | 20 (mM) | pH7.9 |
2 | 1 | drop | 150 (mM) | ||
3 | 1 | drop | TCEP | 0.25 (mM) | |
4 | 1 | drop | protein | 18 (mg/ml) | |
5 | 1 | reservoir | ammonium sulfate | 2.4 (M) | |
6 | 1 | reservoir | CHES | 0.1 (M) | pH9.0 |