4MFD
Structure of the carboxyl transferase domain from Rhizobium etli pyruvate carboxylase with oxalate
X-RAY DIFFRACTION
Starting Model(s)
Initial Refinement Model(s) | |||
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Type | Source | Accession Code | Details |
experimental model | PDB | 4JX4 | PDB ENTRY 4JX4 |
Crystallization
Crystalization Experiments | ||||
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ID | Method | pH | Temperature | Details |
1 | BATCH CRYSTALLIZATION UNDER OIL | 6 | 298 | 11.3% (w/v) PEG 8000, 99 mM BisTris (pH 6.0), 346 mM tetramethylammonium chloride, BATCH CRYSTALLIZATION UNDER OIL, temperature 298K |
Crystal Properties | |
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Matthews coefficient | Solvent content |
2.95 | 58.28 |
Crystal Data
Unit Cell | |
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Length ( Å ) | Angle ( ˚ ) |
a = 85.657 | α = 90 |
b = 157.368 | β = 90 |
c = 244.827 | γ = 90 |
Symmetry | |
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Space Group | P 21 21 21 |
Diffraction
Diffraction Experiment | ||||||||||||||
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ID # | Crystal ID | Scattering Type | Data Collection Temperature | Detector | Detector Type | Details | Collection Date | Monochromator | Protocol | |||||
1 | 1 | x-ray | 100 | CCD | MARMOSAIC 300 mm CCD | 2012-03-31 | M | SINGLE WAVELENGTH |
Radiation Source | |||||
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ID # | Source | Type | Wavelength List | Synchrotron Site | Beamline |
1 | SYNCHROTRON | APS BEAMLINE 21-ID-G | 0.979 | APS | 21-ID-G |
Data Collection
Overall | |||||||||||||||||||
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ID # | Resolution (High) | Resolution (Low) | Percent Possible (Observed) | R Merge I (Observed) | Net I Over Average Sigma (I) | Redundancy | Number Reflections (All) | Number Reflections (Observed) | Observed Criterion Sigma (F) | Observed Criterion Sigma (I) | B (Isotropic) From Wilson Plot | ||||||||
1 | 2.55 | 50 | 99.8 | 0.086 | 21.1 | 7.3 | 108391 | 108188 | -3 | 51.2 |
Highest Resolution Shell | |||||||||||||||||||
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ID # | Resolution (High) | Resolution (Low) | Percent Possible (All) | Percent Possible (Observed) | R Merge I (Observed) | Mean I Over Sigma (Observed) | Redundancy | Number Unique Reflections (All) | |||||||||||
1 | 2.55 | 2.59 | 99.3 | 0.437 | 4.4 | 7.1 |
Refinement
Statistics | |||||||||||||||||||
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Diffraction ID | Structure Solution Method | Cross Validation method | Starting model | Resolution (High) | Resolution (Low) | Number Reflections (Observed) | Number Reflections (R-Free) | Percent Reflections (Observed) | R-Factor (Observed) | R-Work | R-Free | R-Free Selection Details | Mean Isotropic B | ||||||
X-RAY DIFFRACTION | MOLECULAR REPLACEMENT | THROUGHOUT | PDB ENTRY 4JX4 | 2.55 | 48.26 | 102898 | 5409 | 99.4 | 0.1952 | 0.19283 | 0.23951 | RANDOM | 75.346 |
Temperature Factor Modeling | ||||||
---|---|---|---|---|---|---|
Anisotropic B[1][1] | Anisotropic B[1][2] | Anisotropic B[1][3] | Anisotropic B[2][2] | Anisotropic B[2][3] | Anisotropic B[3][3] | |
8.57 | -4.64 | -3.93 |
RMS Deviations | |
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Key | Refinement Restraint Deviation |
r_dihedral_angle_2_deg | 35.247 |
r_dihedral_angle_4_deg | 19.435 |
r_dihedral_angle_3_deg | 16.028 |
r_dihedral_angle_1_deg | 6.617 |
r_long_range_B_refined | 5.74 |
r_long_range_B_other | 5.738 |
r_scangle_other | 2.634 |
r_mcangle_it | 2.617 |
r_mcangle_other | 2.617 |
r_scbond_it | 2.341 |
Non-Hydrogen Atoms Used in Refinement | |
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Non-Hydrogen Atoms | Number |
Protein Atoms | 17794 |
Nucleic Acid Atoms | |
Solvent Atoms | 190 |
Heterogen Atoms | 48 |
Software
Software | |
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Software Name | Purpose |
MD2 | data collection |
PHASER | phasing |
REFMAC | refinement |
DENZO | data reduction |
SCALEPACK | data scaling |