1AMH

UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995-12
Detector	RIGAKU
Spacegroup name	P 1 21 1
Unit cell lengths	45.920, 49.790, 89.880
Unit cell angles	90.00, 97.34, 90.00

Refinement procedure

Resolution	100.000 - 2.500
R-factor	0.182
Rwork	0.182
R-free	0.24200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1brb
RMSD bond length	0.007
RMSD bond angle	26.170 *
Data reduction software	bioteX
Data scaling software	bioteX
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	2.600
High resolution limit [Å]	2.520	2.540 *
Rmerge	0.120	0.296
Number of reflections	13312	470 *
<I/σ(I)>	7.7	2.63
Completeness [%]	94.5	91.9
Redundancy	3.1	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.6	4 *	CRYSTALLIZED AT 277 K FROM 10 MG/ML PROTEIN SOLUTION USING 22% PEG 3350, 10 MM CACL2 AND 0.15M NH4CL AS PRECIPITANT AT PH=5.6 (0.1 M SODIUM CITRATE).

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	sodium citrate	0.1 (M)
3	1	reservoir		10 (mM)
4	1	reservoir	PEG3350	22 (%)
5	1	reservoir	ammonium chloride	0.15 (M)