1IPS
ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)
Experimental procedure
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID2 |
Synchrotron site | ESRF |
Beamline | ID2 |
Temperature [K] | 290 |
Detector technology | IMAGE PLATE |
Collection date | 1994-09 |
Detector | MAR scanner 300 mm plate |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.200, 127.000, 139.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.500 |
R-factor | 0.22 |
Rwork | 0.220 |
R-free | 0.26500 |
Structure solution method | MIR |
RMSD bond length | 0.010 |
RMSD bond angle | 24.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 24.500 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.125 | 0.379 |
Total number of observations | 136252 * | |
Number of reflections | 36775 | |
<I/σ(I)> | 17.6 | 6.8 |
Completeness [%] | 98.6 | 96.7 |
Redundancy | 2.3 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | 18 * | used to seeding, Roach, P.L., (1995) Protein Sci., 4, 1007. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | PEG8000 | 24 (%) | |
2 | 1 | drop | 5 (mM) | ||
3 | 1 | drop | Tris-HCl | 100 (mM) | |
4 | 1 | reservoir | Tris-HCl | 100 (mM) | |
5 | 1 | reservoir | PEG8000 | 16 (%) |