1AHN

E. COLI FLAVODOXIN AT 2.6 ANGSTROMS RESOLUTION

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	140
Detector technology	AREA DETECTOR
Collection date	1995-10
Detector	XUONG-HAMLIN MULTIWIRE
Spacegroup name	P 3 1 2
Unit cell lengths	78.830, 78.830, 52.070
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	10.000 - 2.600
R-factor	0.191 *
Rwork	0.190
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	25.000 *
Data reduction software	SDMS
Data scaling software	SDMS
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.760
High resolution limit [Å]	2.600	2.600
Rmerge	0.064 *	0.190 *
Total number of observations	56473 *
Number of reflections	5995
<I/σ(I)>	17.4	3.8
Completeness [%]	99.5	98.5
Redundancy	9.4	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7	22 *	PROTEIN WAS CRYSTALLIZED IN 30% MPD, 100 MM CACL2, 200 MM PIPES BUFFER, PH 7.0, 295 K.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7.5 (mg/ml)
2	1	drop	MPD	15 (%)
3	1	drop		50 (mM)
4	1	drop	PIPES	100 (mM)
5	1	reservoir	MPD	30 (%)
6	1	reservoir		100 (mM)
7	1	reservoir	PIPES	200 (mM)