4L0R
Crystal structure of FGF2-interacting protein from Homo sapiens. Northeast Structural Genomics Consortium Target HR9027A.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-04-12 |
| Detector | ADSC QUANTUM 4r |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 117.121, 70.097, 31.331 |
| Unit cell angles | 90.00, 94.81, 90.00 |
Refinement procedure
| Resolution | 34.040 - 2.490 |
| R-factor | 0.22441 |
| Rwork | 0.222 |
| R-free | 0.26660 |
| Structure solution method | SAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.286 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHELXS |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.095 | 0.290 |
| Number of reflections | 8351 | |
| <I/σ(I)> | 11.1 | |
| Completeness [%] | 95.9 | 79.3 |
| Redundancy | 5.3 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Microbatch under oil | 6 | 293 | 0.1 M KAcetate, 0.1 M MES, PEG 1000 40% (w/v), pH 6, Microbatch under oil, temperature 293K |
