3BUA
Crystal Structure of TRF2 TRFH domain and APOLLO peptide complex
Experimental procedure
| 実験手法 | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Detector technology | CCD |
| Collection date | 2007-02-08 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97869 |
| Spacegroup name | P 32 2 1 |
| 格子定数 [Å] | 109.947, 109.947, 130.830 |
| 格子定数 [度] | 90.00, 90.00, 120.00 |
精密化法
| 残基 | 50.000 - 2.500 |
| Rwork | 0.229 |
| R-free | 0.25440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h6p |
| 結合長の平均二乗偏差(RMSD) [Å] | 0.006 |
| 結合角の平均二乗偏差(RMSD) [度] | 1.628 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | CNS (1.1) |
Quality characteristics
| Overall | Outer shell | |
| 分解能 [Å] (低) | 50.000 | 2.590 |
| 分解能 [Å] (高) | 2.500 | 2.500 |
| Rmerge_l_obs | 0.086 | 0.610 |
| 独立反射数 | 31885 | |
| <I/σ(I)> | 30 | 2.51 |
| 完全性 [%] | 99.9 | 99.2 |
| 冗長性 | 10.8 | 8 |
結晶化条件
| 結晶ID | 方法 | pH | 温度 | 溶液条件 |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 289 | (NH4)2SO4 2.6 M DTT 1 mM MES 0.05 M pH 5.6 MgAc2 10 mM, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
