1UFH
Structure of putative acetyltransferase, YYCN protein of Bacillus subtilis
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 5ID-B |
Synchrotron site | APS |
Beamline | 5ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-04-20 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9792, 0.9565 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 87.260, 88.580, 55.800 |
Unit cell angles | 90.00, 98.80, 90.00 |
Refinement procedure
Resolution | 26.080 - 2.200 |
R-factor | 0.2339 |
Rwork | 0.233 |
R-free | 0.25900 * |
Structure solution method | MAD |
RMSD bond length | 0.012 |
RMSD bond angle | 1.260 * |
Data scaling software | XDS |
Phasing software | SHARP |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 26.080 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.085 * | 0.238 * |
Number of reflections | 21192 * | |
<I/σ(I)> | 6.8 | 18.8 |
Completeness [%] | 99.3 | 99.3 |
Redundancy | 3.8 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 22 * | 900mM Ammonium phosphate, 190mM Sodium chloride, 100mM Imidazole, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | reservoir | ammonium phosphate | 900 (mM) | |
3 | 1 | reservoir | 190 (mM) | ||
4 | 1 | reservoir | imidazole | 100 (mM) | pH8.0 |