1B2K

Structural effects of monovalent anions on polymorphic lysozyme crystals

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1992-12-01
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	27.730, 62.790, 59.840
Unit cell angles	90.00, 90.10, 90.00

Refinement procedure

Resolution	8.000 - 1.600
R-factor	0.198
Rwork	0.198
R-free	0.23700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	193l
RMSD bond length	0.004
RMSD bond angle	1.170 *
Data reduction software	MOSFLM
Data scaling software	Agrovata
Phasing software	AMoRE
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	13.300	1.640
High resolution limit [Å]	1.600	1.600
Rmerge	0.095 *	0.500 *
Number of reflections	26152
<I/σ(I)>	5.2	1.3
Completeness [%]	96.7	95.6
Redundancy	3.1	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.5	291	pH is adjusted to 4.5 with HI, drop consists of equal volume of protein and reservoir solutions *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	50 (mg/ml)
2	1	reservoir		0.14 (M)