2QRL

Crystal Structure of Oxalylglycine-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2007-05-01
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	64.762, 74.301, 74.619
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 1.600
R-factor	0.209
Rwork	0.208
R-free	0.24100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2Q99 (BACKBONE ONLY)
RMSD bond length	0.013
RMSD bond angle	1.328
Data reduction software	d*TREK
Data scaling software	d*TREK (9.6D)
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.700	29.700	1.660
High resolution limit [Å]	1.600	3.450	1.600
Rmerge	0.056	0.029	0.358
Total number of observations		34590	22894
Number of reflections	46497
<I/σ(I)>	15.8	49.3	3.5
Completeness [%]	96.5	99.3	87.6
Redundancy	6.36	6.71	5.49

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	277	PEG-MME 2000, Tris, AMP, Oxalylglycine, DTT, pH 8.0, vapor diffusion, hanging drop, temperature 277K