1CT5
CRYSTAL STRUCTURE OF YEAST HYPOTHETICAL PROTEIN YBL036C-SELENOMET CRYSTAL
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-11-12 |
Detector | BRANDEIS |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 49.052, 65.823, 93.052 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 12.500 - 2.000 |
R-factor | 0.196 * |
Rwork | 0.196 |
R-free | 0.24500 |
Structure solution method | MAD |
RMSD bond length | 0.015 |
RMSD bond angle | 0.035 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASES |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.067 | 0.253 |
Total number of observations | 138645 * | |
Number of reflections | 20510 | |
<I/σ(I)> | 7.7 | |
Completeness [%] | 97.5 | 94.9 |
Redundancy | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 * | 298 | 30% PEG 4000, 0.1M sodium citrate, 0.2M ammonium acetate, 2.9 mg/ml protein in 6.25mM HEPES and 62.5mM NaCl, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
3 | 1 | reservoir | sodium acetate | 0.2 (M) | |
4 | 1 | reservoir | mPEG2000 | 30 (%) |