3LBF
Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli
Experimental procedure
| 実験手法 | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 100 |
| Collection date | 2009-10-28 |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 |
| 格子定数 [Å] | 52.300, 55.060, 67.490 |
| 格子定数 [度] | 74.00, 74.70, 85.57 |
精密化法
| 残基 | 25.000 - 1.800 |
| R因子 | 0.2151 |
| Rwork | 0.213 |
| R-free | 0.24720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2yxe |
| 結合長の平均二乗偏差(RMSD) [Å] | 0.012 |
| 結合角の平均二乗偏差(RMSD) [度] | 1.240 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Quality characteristics
| Overall | Outer shell | |
| 分解能 [Å] (低) | 25.000 | 1.900 |
| 分解能 [Å] (高) | 1.800 | 1.800 |
| Rmerge_l_obs | 0.056 | 0.207 |
| 独立反射数 | 62259 | |
| <I/σ(I)> | 10.7 | 3.9 |
| 完全性 [%] | 96.2 | |
| 冗長性 | 2.8 | 2.8 |
結晶化条件
| 結晶ID | 方法 | pH | 温度 | 溶液条件 |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 288 | Hepes-Na, monosodium dihydrogen phosphate, monopotassium dihydrogen phosphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K |
