2OQA
X-ray Sequence and Crystal Structure of Luffaculin 1, a Novel Type 1 Ribosome-inactivating Protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-05-22 |
| Detector | MAR CCD 130 mm |
| Wavelength(s) | 1.05 |
| Spacegroup name | P 1 |
| Unit cell lengths | 39.135, 46.813, 83.571 |
| Unit cell angles | 89.07, 80.01, 72.14 |
Refinement procedure
| Resolution | 33.900 - 1.400 |
| R-factor | 0.21313 |
| Rwork | 0.213 |
| R-free | 0.23157 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | a homology model built based on the sequence luffin a |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.153 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.900 | 1.436 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.030 | 0.030 |
| Number of reflections | 94795 | |
| <I/σ(I)> | 21.8 | 4.6 |
| Completeness [%] | 86.7 | 62 |
| Redundancy | 1.9 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 298 | 28% (w/v) PEG 6000, 0.1M citrate buffer(containing 0.02% (w/v) sodium azide)', pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
