1GCU

CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44B2
Synchrotron site	SPring-8
Beamline	BL44B2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-03-20
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	58.682, 70.487, 87.866
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.700 - 1.400
R-factor	0.219
Rwork	0.219
R-free	0.24800
RMSD bond length	0.013
RMSD bond angle	1.600
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	SHARP
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.710	1.480
High resolution limit [Å]	1.400	1.400
Rmerge	0.079	0.324
Total number of observations	379020 *
Number of reflections	71182 *
<I/σ(I)>	6
Completeness [%]		94.3
Redundancy	5.3	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	283	(NH4)2SO4, Na citrate, Na/K tartrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 283K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium citrate	0.1 (M)
2	1	reservoir	potassium sodium tartrate	0.2 (M)
3	1	reservoir	ammonium sulfate	2.0 (M)
4	1	drop	protein	4.3 (mg/ml)