X-RAY DIFFRACTION

Crystallization Details
Method pH Temprature Details
X-RAY DIFFRACTION 6.5 300 15 mg/ml protein concentration, 0.1M Bis-Tris pH 6.5, 0.15M MgCl2, 30% PEG 3350, 10 mM glutamate, 10 mM CoA, acetylornithine soak for 40 minutes; crystal cryoprotected with 25% ethylene glycol
Unit Cell:
a: 168.700 Å b: 55.680 Å c: 81.300 Å α: 90.00° β: 94.30° γ: 90.00°
Symmetry:
Space Group: C 1 2 1
Crystal Properties:
Matthew's Coefficient: 2.18 Solvent Content: 43.46
Refinement Statistics
Diffraction ID Structure Solution Method Cross Validation Method Resolution Limit (High) Resolution Limit (Low) Number of Reflections (Observed) Number of Reflections (R-free) Percent Reflections (Observed) R-Work R-Free Mean Isotropic
X-RAY DIFFRACTION MOLECULAR REPLACEMENT THROUGHOUT 1.45 44.76 127272 2100 97.05 0.11257 0.13601 19.385
Data Collection
Overall
Resolution Limit (High) Resolution Limit (Low) Percent Possible (Observed) R Merge I (Observed) R Sym 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
1.45 44.76 97.0 0.040 ? 20.32 4.4 ? 129373 ? ? ?
Highest Resolution Shell
# Resolution Limits (Low) Resolution Limits (High) Percent Possible (All) Percent Possible (Observed) R-Sym I (Observed) Mean I Over Sigma (Observed) Redundancy Number Unique Reflections (All)
1 1.45 1.54 ? ? ? ? ? ?
Diffraction
Diffraction experiment
Crystal ID Scattering Type Data Collection Temprature Detector Detector Type Details Collection Date Monochromator Protocol
1 100 K ?
Radiation Source
Source Type Wavelength List Synchrotron Site Beamline
SYNCHROTRON MAX IV BEAMLINE BioMAX 0.729 MAX IV BioMAX
Software
Software Name Purpose Version
REFMAC refinement 5.8.0430
PDB_EXTRACT data extraction .
XDS data reduction .
XDS data scaling .
PHASER phasing .
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