5E9Z

Cytochrome P450 BM3 mutant M11

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]	150
Detector technology	CCD
Collection date	2010-01-27
Detector	ADSC QUANTUM 315
Wavelength(s)	1.0
Spacegroup name	C 1 2 1
Unit cell lengths	379.122, 59.720, 95.587
Unit cell angles	90.00, 95.67, 90.00

Refinement procedure

Resolution	95.120 - 2.230
R-factor	0.1895
Rwork	0.188
R-free	0.22530
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ekb
RMSD bond length	0.010
RMSD bond angle	1.090
Data scaling software	SCALA (3.3.15)
Phasing software	PHASER (2.1.4)
Refinement software	BUSTER-TNT

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	95.120	95.119	2.340
High resolution limit [Å]	2.220	7.010	2.220
Rmerge		0.037	0.498
Rmeas	0.114
Rpim	0.062	0.025	0.509
Total number of observations	328643	11421	37951
Number of reflections	101826
<I/σ(I)>	9.1	22.7	2.2
Completeness [%]	96.1	94.4	92.1
Redundancy	3.2	3.4	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	295	Prior to the crystallization setup, 3mM of DTT was added to the concentrated M11 protein sample. Crystals were grown using hanging drops mixing 0.5 uL of M11 with 0.5 uL of the reservoir solution containing 10-15% PEG 3350, 0.1M Tris pH8.0, 0.1-0.2 M MgCl2 or MgSO4, and 10 mM DTT