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 method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2015-07-20
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 21 21 2
Unit cell lengths	78.367, 117.896, 40.256
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.470 - 2.100
R-factor	0.17603
Rwork	0.175
R-free	0.19745
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ea3
RMSD bond length	0.011
RMSD bond angle	1.497
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.140
High resolution limit [Å]	2.100	2.100
Rmerge	0.074	0.599
Number of reflections	22646
<I/σ(I)>	25.6	3.5
Completeness [%]	99.9	100
Redundancy	7.2	6.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	295	Protein: 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%)