1RPM

HUMAN RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU, DOMAIN 1

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX7.2
Synchrotron site	SRS
Beamline	PX7.2
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-04
Detector	MAR scanner 300 mm plate
Spacegroup name	P 1 21 1
Unit cell lengths	95.538, 36.292, 95.381
Unit cell angles	90.00, 95.66, 90.00

Refinement procedure

Resolution	8.000 - 2.300
R-factor	0.195
Rwork	0.195
R-free	0.26000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1yfo
RMSD bond length	0.008
RMSD bond angle	1.390
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	X-PLOR (3.820)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000 *	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.030 *
Total number of observations	112065 *
Number of reflections	26733
<I/σ(I)>	25.2
Completeness [%]	90.0	92
Redundancy	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	5.5	4 *	PROTEIN WAS CRYSTALLIZED FROM 750 MM SODIUM CITRATE, PH 5.5, 2 MM DTT, 0.5 MM EDTA

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7.5 (mg/ml)
2	1	reservoir	sodium cirtate	750 (mM)	pH5.5
3	1	reservoir	dithiothreitol	2 (mM)
4	1	reservoir	EDTA	0.5 (mM)