1IEE

STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME AT 0.94 A FROM CRYSTALS GROWN BY THE COUNTER-DIFFUSION METHOD

Summary for 1IEE

• Entry DOI: 10.2210/pdb1iee/pdb
• Related: 193L 194L 1LSA
• Descriptor: LYSOZYME C, SODIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: lysozyme, 1, 4-beta-n-acetylmuramidase c, hydrolase
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 14531.41

Authors

Sauter, C.,Otalora, F.,Gavira, J.-A.,Vidal, O.,Giege, R.,Garcia-Ruiz, J.-M. (deposition date: 2001-04-09, release date: 2001-08-08, Last modification date: 2023-08-09)

Primary citation

Sauter, C.,Otalora, F.,Gavira, J.A.,Vidal, O.,Giege, R.,Garcia-Ruiz, J.M.
Structure of tetragonal hen egg-white lysozyme at 0.94 A from crystals grown by the counter-diffusion method.
Acta Crystallogr.,Sect.D, 57:1119-1126, 2001

PubMed Abstract: Very high quality crystals of tetragonal hen egg-white lysozyme were grown in the Advanced Protein Crystallization Facility (APCF) on board the Space Shuttle using a modified free-interface diffusion (FID) reactor designed ad hoc to have a longer diffusion path. This design allows the performance of true counter-diffusion experiments. Crystals were obtained under the classical chemical conditions defined 50 y ago with NaCl as a crystallizing agent and acetate pH 4.5 as a buffer. Counter-diffusion crystallization allows a "physical" instead of chemical optimization of growth conditions: indeed, this method screens for the best supersaturation conditions in a single trial and yields crystals of very high quality. A complete diffraction data set was collected at atomic resolution from one of these crystals using synchrotron radiation at the DESY-EMBL beamlines. The overall R(merge) on intensities in the resolution range 31-0.94 A was 5.2% and the data were 98.9% complete. Refinement was carried out with the programs CNS and SHELX97 to a final crystallographic R factor of 12.26% for 72 390 reflections. A mean standard uncertainty in the atomic positions of 0.024 A was estimated from inversion of blocked least-squares matrices. 22 side chains show alternate conformations and the loop 59-75 adopts in the same crystal packing two conformations that were observed for either triclinic or tetragonal lysozyme in previous high-resolution studies. In addition to 255 water molecules, the crystallizing agent (one hexacoordinated sodium ion and five chloride anions) participates in the ordered lysozyme hydration shell.

PubMed: 11468395
DOI: 10.1107/S0907444901008873

Experimental method

X-RAY DIFFRACTION (0.94 Å)