4N17
Crystal structure of a TRAP periplasmic solute binding protein from Burkholderia ambifaria (BAM_6123), Target EFI-510059, With bound beta-D-galacturonate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2013-09-17 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.54 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 96.152, 101.369, 55.720 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.415 - 1.501 |
R-factor | 0.1719 |
Rwork | 0.170 |
R-free | 0.20150 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4lnm |
RMSD bond length | 0.015 |
RMSD bond angle | 1.338 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | HKL-3000 |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 100.000 | 100.000 | 1.530 |
High resolution limit [Å] | 1.500 | 4.070 | 1.500 |
Rmerge | 0.070 | 0.040 | 0.588 |
Number of reflections | 43587 | ||
<I/σ(I)> | 12 | ||
Completeness [%] | 99.4 | 98.9 | 91.8 |
Redundancy | 8 | 8.5 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 59.1 mg/mL protein in 10 mM HEPES, pH 7.5, 5 mM DTT, 10 mM D-galacturonic acid, reservoir: 0.2 M calcium acetate, 0.1 M MES, pH 6.0, 20% w/v PEG8000 (MCSG1 B6), cryoprotection: 4:1 50% w/v PEG3350:reservoir, VAPOR DIFFUSION, SITTING DROP, temperature 298K |