2VFN

Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.1
Synchrotron site	BESSY
Beamline	14.1
Temperature [K]	100
Detector technology	CCD
Collection date	2007-05-02
Detector	MARRESEARCH
Spacegroup name	P 21 3
Unit cell lengths	120.437, 120.437, 120.437
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.150 - 1.500
R-factor	0.128
Rwork	0.127
R-free	0.15500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2vfq
RMSD bond length	0.010
RMSD bond angle	1.338
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.700
High resolution limit [Å]	1.590	1.590
Rmerge	0.050	0.100
Number of reflections	76620
<I/σ(I)>	34.9	10.2
Completeness [%]	98.1	90.5
Redundancy	12.9	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		10		DROP: 2 MICROLITER 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0, PLUS 3.3 MICROLITER, 10 MG/ML PROTEIN SOLUTION IN 10 MM HEPES, PH 7.0; RESERVOIR: 750 MICOLITER 1.0 M AMMONIUM SULFATE, 0.1 M SODIUM PHOSPHATE, PH 10.0