1NB9

Crystal Structure of Riboflavin Kinase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-09-05
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 31 2 1
Unit cell lengths	56.957, 56.957, 82.501
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 * - 1.700
R-factor	0.18476
Rwork	0.184
R-free	0.20600 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1nb0
RMSD bond length	0.016
RMSD bond angle	1.720 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	REFMAC (5.1.27)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.030 *	0.263 *
Total number of observations	251797 *
Number of reflections	17151 *
<I/σ(I)>	42.2	5.1
Completeness [%]	97.5	90.3
Redundancy	7.2	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	20 *	Na cadodalyte, Mg acetate, PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15-17 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)
3	1	drop		300 (mM)
4	1	drop	dithiothreitol	1 (mM)	pH7.2-7.4
5	1	reservoir	sodium cacodylate	100 (mM)	pH6.5
6	1	reservoir	magnesium acetate	200 (mM)
7	1	reservoir	PEG8000	23 (%)