2QH1

Structure of TA289, a CBS-rubredoxin-like protein, in its Fe+2-bound state

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2007-03-20
Detector	RIGAKU RAXIS IV
Spacegroup name	P 21 21 21
Unit cell lengths	58.806, 63.031, 97.474
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.670 - 2.000
R-factor	0.202
Rwork	0.202
R-free	0.23700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1pvm
RMSD bond length	0.006
RMSD bond angle	1.300
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.081	0.340
Number of reflections	24893
<I/σ(I)>	52.7	13.6
Completeness [%]	98.8	97.4
Redundancy	10	10.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.8	298	crystals were grown in a 1:1 solution of protein to resevoir containing 0.1 M Tris HCl (pH 7.8), 0.2 M ammonium formate, 20 % PEG 3350, and 8 % glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K