3EMM

X-ray structure of protein from Arabidopsis thaliana AT1G79260 with Bound Heme

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2008-07-19
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 21 21 2
Unit cell lengths	59.749, 79.732, 36.971
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.836 - 1.358
R-factor	0.171
Rwork	0.170
R-free	0.19800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2a13
RMSD bond length	0.010
RMSD bond angle	1.354
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.410
High resolution limit [Å]	1.358	2.930	1.360
Rmerge	0.041	0.031	0.236
Number of reflections	37822
<I/σ(I)>	22.969		5.074
Completeness [%]	97.2	85.5	97.6
Redundancy	4.7	4.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	277	Protein Solution (16.5 mg/mL native protein [Heme was added in purification step], 0.050 M sodium chloride, 0.0003 M TCEP, 0.005 M MES pH 6.0) mixed in a 1:1 ratio with the Well Solution (24% PEG 4K, 0.05 M BTP pH 7.0 ) Cryoprotected with 30% PEG 4K, 0.05 M BTP pH 7.0 and 15% ethylene glycol, vapor diffusion, hanging drop, temperature 277K, VAPOR DIFFUSION, HANGING DROP