1UW1
A Novel ADP- and Zinc-binding fold from function-directed in vitro evolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-11-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 71.077, 71.077, 54.883 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.940 |
| R-factor | 0.199 * |
| Rwork | 0.200 |
| R-free | 0.22840 * |
| Structure solution method | MAD |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.700 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.000 |
| High resolution limit [Å] | 1.940 | 1.940 |
| Rmerge | 0.069 | 0.477 |
| Total number of observations | 108633 * | |
| Number of reflections | 12124 | |
| <I/σ(I)> | 32 | 7.3 |
| Completeness [%] | 99.5 | 99.3 |
| Redundancy | 9 | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 * | USING THE HANGING-DROP VAPOR DIFFUSION TECHIQUE. 20MG/ML OF PROTEIN WAS MIXED IN EQUAL VOLUMES WITH A CRYSTALLIZATION BUFFER OF 0.1M TRIS/HCL PH 8.5, 0.2 M SODIUM CITRATE, 30% PEG 400) |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | add | protein | 20 (mg/ml) | |
| 2 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
| 3 | 1 | reservoir | sodium citrate | 0.2 (M) | |
| 4 | 1 | reservoir | PEG400 | 30 (%) |
