1O58

Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.80 A resolution

Replaces:  1J6N

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-2
Synchrotron site	SSRL
Beamline	BL9-2
Temperature [K]	100
Detector technology	CCD
Collection date	2001-12-10
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97999, 0.97980, 0.91837
Spacegroup name	P 1 21 1
Unit cell lengths	67.570, 84.590, 107.220
Unit cell angles	90.00, 95.39, 90.00

Refinement procedure

Resolution	48.660 - 1.800
R-factor	0.15938
Rwork	0.157
R-free	0.19800 *
Structure solution method	MAD
RMSD bond length	0.017
RMSD bond angle	1.410 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MLPHARE
Refinement software	REFMAC (5.1.9999)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.800 *	1.850
High resolution limit [Å]	1.800	1.800
Rmerge	0.038 *	0.273 *
Total number of observations	400214 *
Number of reflections	97122
<I/σ(I)>	20.2	4.3
Completeness [%]	87.6	69.7 *
Redundancy	4.1	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.9 *	293	50% PEG-400, 0.1M CHES pH 9.5, 0.2M NaCl, pH 9.2, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	Tris	20 (mM)	pH7.9
2	1	reservoir		150 (mM)
3	1	reservoir	TCEP	0.25
4	1	drop	protein	13 (mg/ml)