1PCZ

STRUCTURE OF TATA-BINDING PROTEIN

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	173
Detector technology	IMAGE PLATE
Collection date	1994-10-04
Detector	FUJI
Spacegroup name	P 61
Unit cell lengths	89.620, 89.620, 141.280
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	6.000 - 2.200
R-factor	0.218
Rwork	0.218
R-free	0.30100 *
Structure solution method	MULTIPLE ISOMORPHOUS REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	1.850 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELXL-96
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.330
High resolution limit [Å]	2.100	2.200
Rmerge	0.079	0.237
Number of reflections	36912
<I/σ(I)>	16.9	4.5
Completeness [%]	98.8	98.6
Redundancy	3.2	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	18 *	50% SATURATED AMMONIUM SULFATE, 0.1 M TRIS PH 7.5, 0.1 M KCL

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	Tris-HCl	100 (mM)
3	1	drop		100 (mM)
4	1	drop	ammonium sulfate	25 (%sat)
5	1	reservoir	Tris-HCl	100 (mM)
6	1	reservoir		100 (mM)
7	1	reservoir	ammonium sulfate	50 (%sat)