3E1P
Crystal structure of E. coli Bacterioferritin (BFR) in which the Ferroxidase centre is inhibited with ZN(II) and high occupancy iron is bound within the cavity.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX10.1 |
Synchrotron site | SRS |
Beamline | PX10.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-01-01 |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 207.397, 207.397, 142.451 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 71.250 - 2.400 |
R-factor | 0.241 |
Rwork | 0.240 |
R-free | 0.26000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2QP7 (APO-BFR) |
RMSD bond length | 0.012 |
RMSD bond angle | 1.433 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 73.320 | 2.530 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 117098 | |
<I/σ(I)> | 16.3 | 3.1 |
Completeness [%] | 97.0 | 83.3 |
Redundancy | 12 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 298 | 1.8 M AMMONIUM SULFATE, 0.1 M TRI- SODIUM CITRATE PH 5. APO-BFR CRYSTALS WERE SUBSEQUENTLY (AEROBICALLY) SOAKED IN A CRYOPROTECTANT SOLUTION CONTAINING FE2+ (AND BUFFERED AT PH 7.0 WITH 0.1 M MOPS IN PLACE OF CITRATE) FOR 65 MINUTES BEFORE FALSH FREEZING AND DATA COLLECTION. PLEASE SEE PAPER FOR FULL DETAILS., PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, pH 5.00 |