3ECF
Crystal structure of an ntf2-like protein (ava_4193) from anabaena variabilis atcc 29413 at 1.90 A resolution
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL11-1 |
| Synchrotron site | SSRL |
| Beamline | BL11-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-08-06 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.91837,0.97864 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 74.056, 74.056, 189.378 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.323 - 1.900 |
| R-factor | 0.184 |
| Rwork | 0.182 |
| R-free | 0.22200 |
| Structure solution method | MAD |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.683 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.5) |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.323 | 29.330 | 1.950 |
| High resolution limit [Å] | 1.900 | 8.500 | 1.900 |
| Rmerge | 0.154 | 0.053 | 0.668 |
| Total number of observations | 3377 | 22422 | |
| Number of reflections | 42557 | ||
| <I/σ(I)> | 4.213 | 7.6 | 1.1 |
| Completeness [%] | 100.0 | 97.6 | 100 |
| Redundancy | 7.2 | 5.8 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 277 | 2.4000M (NH4)2SO4, 0.1M MES pH 6.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K |






