1CT5

CRYSTAL STRUCTURE OF YEAST HYPOTHETICAL PROTEIN YBL036C-SELENOMET CRYSTAL

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	CCD
Collection date	1998-11-12
Detector	BRANDEIS
Spacegroup name	P 21 21 21
Unit cell lengths	49.052, 65.823, 93.052
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	12.500 - 2.000
R-factor	0.196 *
Rwork	0.196
R-free	0.24500
Structure solution method	MAD
RMSD bond length	0.015
RMSD bond angle	0.035
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASES
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.067	0.253
Total number of observations	138645 *
Number of reflections	20510
<I/σ(I)>	7.7
Completeness [%]	97.5	94.9
Redundancy	6.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6 *	298	30% PEG 4000, 0.1M sodium citrate, 0.2M ammonium acetate, 2.9 mg/ml protein in 6.25mM HEPES and 62.5mM NaCl, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	ammonium sulfate	0.2 (M)
3	1	reservoir	sodium acetate	0.2 (M)
4	1	reservoir	mPEG2000	30 (%)