2C7I

Structure of protein Ta0514, putative lipoate protein ligase from T. acidophilum.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	CCD
Detector	ADSC CCD
Spacegroup name	P 1 21 1
Unit cell lengths	53.230, 118.356, 105.592
Unit cell angles	90.00, 93.75, 90.00

Refinement procedure

Resolution	19.870 - 2.100
R-factor	0.21
Rwork	0.208
R-free	0.25200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	SEE REMARK
RMSD bond length	0.010
RMSD bond angle	1.254
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.870	2.170
High resolution limit [Å]	2.100	2.080
Rmerge	0.070	0.230
Number of reflections	68335
<I/σ(I)>	22	6
Completeness [%]	95.3	72.3
Redundancy	10

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		6.7		pH 6.70