3FWY

Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein

Replaces:  3END

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-2
Synchrotron site	SSRL
Beamline	BL9-2
Temperature [K]	100
Detector technology	CCD
Collection date	2008-01-19
Detector	MARMOSAIC 325 mm CCD
Wavelength(s)	0.98000
Spacegroup name	P 21 21 21
Unit cell lengths	56.729, 86.622, 117.169
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.020 - 1.630
R-factor	0.17529
Rwork	0.174
R-free	0.19860
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2nip
RMSD bond length	0.008
RMSD bond angle	1.206
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.670
High resolution limit [Å]	1.630	1.630
Number of reflections	133747
<I/σ(I)>	40	4.6
Completeness [%]	96.4	93.83
Redundancy	2	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	CAPILLARY BATCH DIFFUSION	7.8	301	20-25% PEG 3350, 200mM Magnesium formate, 10mM MgADP, pH 7.8, CAPILLARY BATCH DIFFUSION, temperature 301K