194L

THE 1.40 A STRUCTURE OF SPACEHAB-01 HEN EGG WHITE LYSOZYME

Summary for 194L

• Entry DOI: 10.2210/pdb194l/pdb
• Descriptor: LYSOZYME, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase (o-glycosyl)
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14389.60

Authors

Vaney, M.C.,Maignan, S.,Ries-Kautt, M.,Ducruix, A. (deposition date: 1995-09-01, release date: 1995-12-07, Last modification date: 2024-10-30)

Primary citation

Vaney, M.C.,Maignan, S.,Ries-Kautt, M.,Ducriux, A.
High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission.
Acta Crystallogr.,Sect.D, 52:505-517, 1996

PubMed Abstract: Crystals of tetragonal hen egg-white lysozyme were grown using Advanced Protein Crystallization Facility (APCF) apparatus under a microgravity environment (SpaceHab-01 mission) and ground control conditions. Crystals were grown from NaCl as a crystallizing agent at pH 4.3. The X-ray diffraction patterns of the best diffracting ground- and space-grown crystals were recorded using synchrotron radiation and an image plate on the W32 beamline at LURE. Both ground- and space-grown crystals showed nearly equivalent maximum resolution of 1.3-1.4 A. Refinements were carried out with the program X-PLOR with final R values of 18.45 and 18.27% for structures from ground- and space- grown crystals, respectively. The two structures are nearly identical with the root-mean-square difference on all protein atoms being 0.13 A. Some residues of the two refined structures show multiple alternative conformations. Two ions were localized into the electron-density maps of the two structures: one chloride ion at the interface between two symmetry-related molecules and one sodium ion stabilizing the loop Ser60-Leu75. The sodium ion is surrounded by six ligands which form a bipyramid around it at distances of 2.2-2.6 A.

PubMed: 15299672
DOI: 10.1107/S090744499501674X

Experimental method

X-RAY DIFFRACTION (1.4 Å)