13EA

X-ray crystal structure of human biliverdin beta IX reductase in complex with NADP and BCT002066

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 17-ID-1
Synchrotron site	NSLS-II
Beamline	17-ID-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-05-24
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.920105
Spacegroup name	C 1 2 1
Unit cell lengths	75.595, 42.117, 66.306
Unit cell angles	90.00, 107.50, 90.00

Refinement procedure

Resolution	31.620 - 1.740
R-factor	0.1746
Rwork	0.173
R-free	0.20730
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.995
Data reduction software	autoPROC
Data scaling software	autoPROC
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.620	1.768
High resolution limit [Å]	1.738	1.738
Rmerge	0.118	1.205
Rmeas	0.137	1.410
Rpim	0.068	0.721
Number of reflections	20461	988
<I/σ(I)>	7.1	1.1
Completeness [%]	98.8
Redundancy	3.9
CC(1/2)	0.996	0.465

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	6.5	291	protein solution: BLVRB at 18 mg/mL in 50 mM Bis-Tris, pH 6.5, 50 mM NaCl, 1 mM DTT, 1 mM NADP+ well solution: 0.1 M MES monohydrate pH 6.5, 10-12% (w/v) PEG 20,000, and 25% (v/v) MPD. Crystallization droplets comprised 0.5 uL protein solution was mixed with 0.5 uL of well solution. BLVRB/NADP+ crystals were soaked for approximately 1 hour in a drop containing 2.5-5 mM BCT2066 (dissolved in 100% DMSO) and vitrified with 30% (v/v) glycerol as cryoprotectant.