1TVF
Crystal Structure of penicillin-binding protein 4 (PBP4) from Staphylococcus aureus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9A |
Synchrotron site | NSLS |
Beamline | X9A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-10-23 |
Detector | MARRESEARCH |
Wavelength(s) | 0.98 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 48.713, 140.189, 145.775 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.680 - 2.000 |
R-factor | 0.166 |
Rwork | 0.166 |
R-free | 0.20500 |
Structure solution method | SIRAS, MOLECULAR REPLACEMENT |
Starting model (for MR) | Arp/Warp autobuilt model using phases from two Ta6Br12 clusters and a poor molecular replacement solution. MR was carried out using a model derived from PDB entry 1HD8 which is a mutant of PBP5 sharing ~26% identity with PBP4 over a 245 residue range. Phase combination with MR solution was necessary as Ta6Br12 clusters occupied positions on the symmetry planes resulting in centrosymmetric phases and hence uninterpretable maps. |
RMSD bond length | 0.024 |
RMSD bond angle | 2.100 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 67865 | |
<I/σ(I)> | 17.1 | 5.5 |
Completeness [%] | 98.9 | 98.7 |
Redundancy | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 291 | 24% PEG 4000, 100mM citrate buffer, 200mM Ammonium Sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 291 | 24% PEG 4000, 100mM citrate buffer, 200mM Ammonium Sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |