2VFQ

Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V450A

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	2006-10-29
Detector	MARRESEARCH
Spacegroup name	P 21 3
Unit cell lengths	119.990, 119.990, 119.990
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 1.550
R-factor	0.116
Rwork	0.114
R-free	0.14500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2vfo
RMSD bond length	0.011
RMSD bond angle	1.213
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	0.040	0.070
Number of reflections	50813
<I/σ(I)>	46.2	23
Completeness [%]	88.9	58.3
Redundancy	10.9	7.7

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