1MRZ

Crystal structure of a flavin binding protein from Thermotoga Maritima, TM379

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	CCD
Collection date	2001-05-02
Detector	ADSC QUANTUM 4
Wavelength(s)	0.97911
Spacegroup name	P 1 21 1
Unit cell lengths	67.211, 83.095, 67.851
Unit cell angles	90.00, 116.93, 90.00

Refinement procedure

Resolution	30.000 * - 1.900
R-factor	0.21696
Rwork	0.217
R-free	0.23300 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	MAD
RMSD bond length	0.007
RMSD bond angle	1.120 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.038 *	0.299 *
Number of reflections	51627 *	2190 *
<I/σ(I)>	27	4.1
Completeness [%]	96.9	82.2
Redundancy	3.8 *	3.5 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	293	0.2M Na Citrate, 23% PEG 3350, 10% Glycerol, pH 7.5, EVAPORATION, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris	20 (mM)	pH7.5
2	1	drop	EDTA	1 (mM)
3	1	drop	glycerol	10 (%)
4	1	drop	protein	21.5 (mg/ml)
5	1	reservoir	sodium citrate	0.2 (mM)
6	1	reservoir	PEG4000	10 (%)
7	1	reservoir	glycerol	5 (%)
8	1	reservoir	propanol	10 (%)