1M7V

STRUCTURE OF A NITRIC OXIDE SYNTHASE HEME PROTEIN FROM BACILLUS SUBTILIS WITH TETRAHYDROFOLATE AND ARGININE BOUND

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	100
Detector technology	CCD
Collection date	2002-05-24
Detector	ADSC QUANTUM 4
Wavelength(s)	0.916
Spacegroup name	P 21 21 2
Unit cell lengths	81.155, 92.553, 62.939
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.800 - 1.940 *
Rwork	0.225
R-free	0.23900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dww
RMSD bond length	0.012 *
RMSD bond angle	1.510 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.980
High resolution limit [Å]	1.940	1.940
Rmerge	0.059 *	0.399 *
Total number of observations	395408 *
Number of reflections	44343
<I/σ(I)>	27.5	2.5
Completeness [%]	99.7	99.7
Redundancy	8.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5 *	22 *	PEG 8K, potassium acetate, pH 7.0, VAPOR DIFFUSION, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	45 (mg/ml)
2	1	drop	THF	33 (mM)
3	1	drop	Tris	50 (mM)	pH7.5
4	1	drop		150 (mM)
5	1	drop	dithiothreitol	2 (mM)
6	1	reservoir	sodium cacodylate	100 (mM)	pH6.0-6.8
7	1	reservoir	potassium acetate	200 (mM)
8	1	reservoir	PEG8000	16-21 (%)