1M4L
STRUCTURE OF NATIVE CARBOXYPEPTIDASE A AT 1.25 RESOLUTION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12B |
| Synchrotron site | NSLS |
| Beamline | X12B |
| Temperature [K] | 297 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-09-01 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 1.085 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.687, 60.267, 47.453 |
| Unit cell angles | 90.00, 97.47, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.250 |
| Rwork | 0.104 |
| R-free | 0.14510 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTERY 1YME |
| RMSD bond length | 0.015 |
| RMSD bond angle | 0.030 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | TNT |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.270 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmerge | 0.066 | 0.127 |
| Number of reflections | 64976 | |
| <I/σ(I)> | 13.5 | |
| Completeness [%] | 86.3 | 36.3 |
| Redundancy | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Microdialysis * | 7.5 * | 5 * | Shoham, G., (1988) Proc.Natl.Acad.Sci.USA., 85, 684. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | 1.0 (M) | ||
| 2 | 1 | 1 | Tris-HCl | 0.03 (M) | pH7.5 |
| 3 | 1 | 2 | 0.2 (M) | ||
| 4 | 1 | 1 | Tris-HCl | 0.03 (M) | pH7.5 |
