1BR9
HUMAN TISSUE INHIBITOR OF METALLOPROTEINASE-2
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 72.050, 52.700, 46.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.100 |
| R-factor | 0.238 * |
| Rwork | 0.238 |
| R-free | 0.27100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | BOVINE TISSUE INHIBITOR FERNANDEZ-CATALAN ET AL. 1998 EMBO J. IN PRESS |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.024 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.200 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.083 | 0.284 |
| Total number of observations | 100589 * | |
| Number of reflections | 10532 | |
| <I/σ(I)> | 15.4 | 4.6 |
| Completeness [%] | 98.8 | 98.5 |
| Redundancy | 10 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | 4 * | pH 8.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-15 (mg/ml) | |
| 2 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
| 3 | 1 | reservoir | 0.1 (M) | ||
| 4 | 1 | reservoir | PEG400 | 30 (%(w/v)) |
