X-RAY DIFFRACTION

Crystallization Details
Method pH Temprature Details
X-RAY DIFFRACTION ? 293 After limited proteolysis with subtilisin A, 7.5 mg/ml target protein were mixed with an equal volume of crystallization solution (10% w/v PEG 10000, 250 mM MgSO4 and 100 mM Tris/HCl pH 9.0)
Unit Cell:
a: 58.260 Å b: 58.260 Å c: 135.380 Å α: 90.000° β: 90.000° γ: 90.000°
Symmetry:
Space Group: P 43 21 2
Crystal Properties:
Matthew's Coefficient: 2.51 Solvent Content: 50.95
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 FREE R-VALUE 2.07 20.60 14863 1486 99.75 0.2076 0.2342 44.77
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
2.07 21.04 100 ? ? 8.5 732.8 ? 14959 ? ? 43.30
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 2.07 2.12 ? ? ? ? ? ?
Diffraction
Diffraction experiment
Crystal ID Scattering Type Data Collection Temprature Detector Detector Type Details Collection Date Monochromator Protocol
1 293 K ?
Radiation Source
Source Type Wavelength List Synchrotron Site Beamline
FREE ELECTRON LASER SLAC LCLS BEAMLINE MFX 1.265 SLAC LCLS MFX
Software
Software Name Purpose Version
PHENIX refinement 2.0-5936_9999
CrystFEL data reduction .
CrystFEL data scaling .
PHENIX phasing .
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