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5CQE

2.1 Angstrom resolution crystal structure of matrix protein 1 (M1; residues 1-164) from Influenza A virus (A/Puerto Rico/8/34(H1N1))

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 21-ID-G
Synchrotron siteAPS
Beamline21-ID-G
Temperature [K]100
Detector technologyCCD
Collection date2015-07-20
DetectorMARMOSAIC 300 mm CCD
Wavelength(s)0.97856
Spacegroup nameP 21 21 2
Unit cell lengths78.367, 117.896, 40.256
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution29.470 - 2.100
R-factor0.17603
Rwork0.175
R-free0.19745
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ea3
RMSD bond length0.011
RMSD bond angle1.497
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwarePHASER
Refinement softwareREFMAC (5.7.0029)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.140
High resolution limit [Å]2.1002.100
Rmerge0.0740.599
Number of reflections22646
<I/σ(I)>25.63.5
Completeness [%]99.9100
Redundancy7.26.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP5295Protein: 12.8 mg/mL 10 mM Tris-HCl pH 8.3 500 mM NaCl 0.5 mM TCEP Crsytallization: The JCSG+ Suite (B9: 100 mM Citric acid pH 4.0 20% (w/v) PEG 6000; final pH 5.0 Cryocondition: Crystallization condition + sucrose (50%)

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