1LC0

Structure of Biliverdin Reductase and the Enzyme-NADH Complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-1
Synchrotron site	SSRL
Beamline	BL9-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-05-01
Detector	MARRESEARCH
Wavelength(s)	0.98
Spacegroup name	P 21 21 21
Unit cell lengths	51.780, 75.730, 76.080
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.000 * - 1.200
Rwork	0.222
R-free	0.23200 *
Structure solution method	MIR
RMSD bond length	0.006
RMSD bond angle	23.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.000 *	1.210
High resolution limit [Å]	1.200	1.200
Rmerge	0.048 *	0.450 *
Total number of observations	636022 *
Number of reflections	95268 *
Completeness [%]	98.1	99.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	10.5	4 *	2.0 M Na+/K+ phosphate, 100 mM CAPS, 200 mM lithium sulfate (Emerald Screen Wizard-I condition 27), pH 10.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6.5 (mg/ml)
2	1	reservoir	sodium potassium phosphate	2.0 (M)
3	1	reservoir	CAPS	100 (mM)	pH10.5
4	1	reservoir	lithium sulfate	200 (mM)