2CN4
The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-10-04 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 47.080, 62.320, 56.820 |
Unit cell angles | 90.00, 105.34, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.300 |
R-factor | 0.172 |
Rwork | 0.169 |
R-free | 0.22400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1b2v |
RMSD bond length | 0.008 |
RMSD bond angle | 1.201 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 55.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.030 | 0.070 |
Number of reflections | 14221 | |
<I/σ(I)> | 18 | 7 |
Completeness [%] | 95.8 | 91.1 |
Redundancy | 1.9 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 2 MICROLITERS PROTEIN (AT A CONCENTRATION OF ABOUT 4 MG/ML) WERE MIXED WITH 1 MICROLITER RESERVOIR CONSISTING OF 100 MM TRIS BUFFER AT PH 8.5, 2 M K2HPO4 AND 2 M NAH2PO4. |