1QLQ

Bovine Pancreatic Trypsin Inhibitor (BPTI) Mutant with Altered Binding Loop Sequence

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	SIEMENS SRA2
Temperature [K]	290
Detector technology	IMAGE PLATE
Collection date	1999-01-15
Detector	MARRESEARCH
Spacegroup name	P 43 21 2
Unit cell lengths	52.710, 52.710, 43.410
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.420
R-factor	0.1048 *
R-free	0.16090
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bpi
RMSD bond length	0.014
RMSD bond angle	0.032
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELXL-97
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.470
High resolution limit [Å]	1.420	1.420
Rmerge	0.059	0.326
Number of reflections	11934
<I/σ(I)>	50.2	5.144
Completeness [%]	99.6	96
Redundancy	19.3	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	19 *	A PROTEIN SAMPLE, LYOPHILIZED AFTER HPLC PURIFICATION FROM TFA/ACETONITRILE MIXTURE, WAS DISSOLVED IN WATER TO A CONCENTRATION OF 9 MG/ML. 2 UL DROPS OF THE PROTEIN SOLUTION WERE MIXED WITH 2 UL OF RESERVOIR SOLUTION CONTAINING 2% PEG 400, 2 M AMMONIUM SULFATE AND 0.1 M NA HEPES, PH 7.5. THE HANGING DROPLETS WERE EQUILIBRATED AT 19 DEG C THROUGH THE GAS PHASE WITH THE RESERVOIR. PRISMATIC CRYSTALS MEASURING UP TO 0.4 MM GREW WITHIN 12 HOURS.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	14 (mg/ml)
2	1	reservoir	PEG400	2 (%)
3	1	reservoir	ammonium sulfate	2.0 (M)
4	1	reservoir	sodium HEPES	0.1 (M)