1AT6

HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-03
Detector	RIGAKU
Spacegroup name	P 43 21 2
Unit cell lengths	76.660, 76.660, 38.290
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 * - 1.800
R-factor	0.184
Rwork	0.184
R-free	0.23000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1lzb
RMSD bond length	0.010
RMSD bond angle	23.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.843)
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	34.300	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.049	0.147
Total number of observations	115484 *
Number of reflections	10515
<I/σ(I)>	39.6	7.1
Completeness [%]	95.8	64.9
Redundancy	11	5.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7.5	4 *	CRYSTALS WERE PREPARED AT 277 K FROM THE DROPLET MIXTURE OF A 20 MG/ML PROTEIN SOLUTION CONTAINING 7 MM TRI-N-ACETYLCHITOTRIOSE (NAG3) AND 50 MM ACETATE BUFFER PH 4.2 WITH EQUAL VOLUME OF A RESERVOIR SOLUTION CONTAINING 2.0 M AMMONIUM FORMATE AND 100 MM N-(2-HYDROXYETHYL)PIPERAZINE-N'-(2-ETHANESULFONIC ACID) (HEPES) BUFFER PH 7.5. PRIOR TO THE DIFFRACTION DATA COLLECTION, THE CRYSTAL WAS SOAKED IN A CRYOPROTECTANT SOLUTION CONTAINING 30 % (W/V) POLYETHYLENE GLYCOL 20,000, 2.2 M AMMONIUM FORMATE, 100 MM HEPES BUFFER PH 7.5, AND 7 MM NAG3 FOR 2 MINUTES AT 277 K.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	NAG3	3.5 (mM)
3	1	drop	sodium acetate	25 (mM)
4	1	drop	ammonium formate	1.0 (M)
5	1	drop	HEPES	50 (mM)
6	1	reservoir	ammonium formate	2.0 (M)
7	1	reservoir	HEPES	100 (mM)