4FXV
Crystal structure of an ELAV-like protein 1 (ELAVL1) from Homo sapiens at 1.90 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL14-1 |
| Synchrotron site | SSRL |
| Beamline | BL14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-01-15 |
| Detector | MARMOSAIC 325 mm CCD |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 73.436, 73.436, 272.957 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.823 - 1.900 |
| R-factor | 0.2032 |
| Rwork | 0.202 |
| R-free | 0.23490 |
| Structure solution method | SAD |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.781 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 28.823 | 28.823 | 1.950 |
| High resolution limit [Å] | 1.900 | 8.500 | 1.900 |
| Rmerge | 0.058 | 0.482 | |
| Rmeas | 0.140 | 0.062 | 0.525 |
| Rpim | 0.044 | 0.020 | 0.199 |
| Total number of observations | 352640 | 4004 | 15252 |
| Number of reflections | 34829 | ||
| <I/σ(I)> | 11.2 | 20.4 | 2.6 |
| Completeness [%] | 97.9 | 95.8 | 87.4 |
| Redundancy | 10.1 | 8.1 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 277 | 0.200M NH4Cl, 20.00% PEG-3350, No Buffer pH 6.3, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
