1N8N
Crystal structure of the Au3+ complex of AphA class B acid phosphatase/phosphotransferase from E. coli at 1.69 A resolution
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-07-13 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0377, 1.0404, 0.9392 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 49.279, 92.457, 138.182 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 * - 1.690 |
R-factor | 0.17906 |
Rwork | 0.178 |
R-free | 0.20700 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | MAD-phased Bromine derivative at 2.2 A resolution |
RMSD bond length | 0.020 * |
RMSD bond angle | 1.400 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 * | 1.790 |
High resolution limit [Å] | 1.690 | 1.690 |
Rmerge | 0.075 * | 0.375 * |
Total number of observations | 135549 * | |
Number of reflections | 31884 | 2579 * |
<I/σ(I)> | 7 | 7 |
Completeness [%] | 98.2 * | 92 * |
Redundancy | 4.3 * | 2.9 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 293 | AphA 6mg/mL, 50 mM Na acetate, 25% PEG 6000, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K. The crystals of the native enzyme (containing Mg2+ or Zn2+) have been soaked in 1 mM solution of AuCl3 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG6000 | 17-22 (%) | |
3 | 1 | reservoir | 1 (mM) |