1LQ2
Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with gluco-phenylimidazole
Experimental procedure
実験手法 | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | MACSCIENCE |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-08-15 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 43 21 2 |
格子定数 [Å] | 100.693, 100.693, 182.676 |
格子定数 [度] | 90.00, 90.00, 90.00 |
精密化法
残基 | 25.000 - 2.620 * |
Rwork | 0.210 |
R-free | 0.27290 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ieq |
結合長の平均二乗偏差(RMSD) [Å] | 0.010 |
結合角の平均二乗偏差(RMSD) [度] | 1.700 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Quality characteristics
Overall | Outer shell | |
分解能 [Å] (低) | 50.000 | 2.690 |
分解能 [Å] (高) | 2.620 | 2.620 |
Rmerge_l_obs | 0.130 | 0.583 * |
Total number of observations | 70377 * | |
独立反射数 | 44625 * | |
<I/σ(I)> | 5.9 | |
完全性 [%] | 73.6 * | 45.4 * |
冗長性 | 1.81 |
結晶化条件
結晶ID | 方法 | pH | 温度 | 溶液条件 |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277-279 * | Hrmova, M., (1998) Acta Cryst., D54, 687. * |
文献の結晶化試薬
ID | 結晶ID | 溶液 | 試薬名 | 濃度 (単位) (単位) | 詳細 |
1 | 1 | drop | enzyme | 6.8 (mg/ml) | |
2 | 1 | drop | HEPES-NaOH | 75 (mM) | |
3 | 1 | drop | sodium acetate | 7.5 (mM) | |
4 | 1 | drop | PEG400 | 1.2 (%(w/v)) | |
5 | 1 | drop | ammonium sulfate | 0.8 (M) | |
6 | 1 | reservoir | ammonium sulfate | 1.7 (M) | |
7 | 1 | reservoir | HEPES-NaOH | 50 (mM) |