1VI7

Crystal structure of an hypothetical protein

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 32-ID
Synchrotron site	APS
Beamline	32-ID
Detector technology	CCD
Detector	MARRESEARCH
Wavelength(s)	0.9795, 0.9795
Spacegroup name	H 3
Unit cell lengths	148.749, 148.749, 35.602
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	37.190 - 2.800
R-factor	0.2591 *
Rwork	0.261
R-free	0.31600 *
Structure solution method	Se-Met MAD phasing
RMSD bond length	0.013
RMSD bond angle	2.400 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	REFMAC (4.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	37.190	2.700
High resolution limit [Å]	2.800 *	2.560
Rmerge	0.104 *	0.485 *
Total number of observations	81478 *
Number of reflections	7231 *
<I/σ(I)>	14.8	4.7
Completeness [%]	100.0	100
Redundancy	11.3	11.3 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	9 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
10	1	reservoir	beta-mercaptoethanol	28.4 (mM)
2	1	drop	beta-mercaptoethanol	1.0 (mM)
3	1	drop		150 (mM)
4	1	drop	HEPES	10 (mM)	pH7.5
5	1	drop	methionine	10 (mM)
6	1	drop	glycerol	10 (%)
7	1	reservoir	MES	150 (mM)	pH6.5
8	1	reservoir	ammonium sulfate	150 (mM)
9	1	reservoir	PEG5000 MME	30 (%)