1E2W

N168F mutant of cytochrome f from Chlamydomonas reinhardtii

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	1999-04-15
Detector	CUSTOM-MADE
Spacegroup name	P 1 21 1
Unit cell lengths	59.030, 81.180, 61.080
Unit cell angles	90.00, 103.52, 90.00

Refinement procedure

Resolution	27.410 - 1.600
R-factor	0.197
Rwork	0.197
R-free	0.22600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1e2v
RMSD bond length	0.005
RMSD bond angle	25.900 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CNS (1.0)
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	27.840	1.660
High resolution limit [Å]	1.600	1.600
Rmerge	0.046	0.378
Total number of observations	277890 *
Number of reflections	73580
<I/σ(I)>	28.6	3.54
Completeness [%]	99.6	100
Redundancy	3.8	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5 *		THE PROTEIN WAS BUFFERED IN 10 MM NA2HPO4/NAH2PO4, PH 7.5, 1 MM DTT, THE RESERVOIR CONTAINED 100 MM MES, PH 6.7, 200 MM AMMONIUM FORMATE, 14% GLYCEROL, 17% PEG-3350.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	dithiothreitol	1 (mM)
3	1	reservoir	MES	100 (mM)
4	1	reservoir	ammonium formate	200 (mM)
5	1	reservoir	glycerol	14 (%)
6	1	reservoir	PEG3350	17 (%)