2X1C
The crystal structure of precursor acyl coenzyme A:isopenicillin N acyltransferase from Penicillium chrysogenum
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-06-20 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 231.225, 68.233, 151.277 |
| Unit cell angles | 90.00, 129.57, 90.00 |
Refinement procedure
| Resolution | 48.800 - 1.850 |
| R-factor | 0.17037 |
| Rwork | 0.169 |
| R-free | 0.19288 |
| Structure solution method | MAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.113 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.920 | 1.950 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.040 | 0.210 |
| Number of reflections | 152842 | |
| <I/σ(I)> | 21.51 | 5.4 |
| Completeness [%] | 98.5 | 98.6 |
| Redundancy | 2.93 | 2.72 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 1.6 M (NH4)2SO4, 0.1 M NACL, 0.1 M HEPES-NAOH, PH 7.5 |
