2OO5

Structure of transhydrogenase (dI.H2NADH)2(dIII.NADP+)1 asymmetric complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Wavelength(s)	0.93100
Spacegroup name	P 21 21 21
Unit cell lengths	71.199, 101.025, 131.721
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	80.060 - 2.600
R-factor	0.222
Rwork	0.219
R-free	0.27500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1u2d
RMSD bond length	0.008
RMSD bond angle	1.252
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	80.163	62.620	2.740
High resolution limit [Å]	2.600	8.220	2.600
Rmerge	0.073	0.050	0.227
Total number of observations		3253	12512
Number of reflections	27548
<I/σ(I)>	7.7	10	3.3
Completeness [%]	92.8	88.8	94.4
Redundancy	3.8	3.5	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	8	277	18% PEG 4000, 10% glycerol, 100mM Tris, 75mM lithium sulphate, VAPOR DIFFUSION, temperature 277K