2ANX

crystal structure of bacteriophage P22 lysozyme mutant L87M

Summary for 2ANX

• Entry DOI: 10.2210/pdb2anx/pdb
• Related: 2ANV
• Descriptor: Lysozyme, SULFATE ION, SAMARIUM (III) ION, ... (6 entities in total)
• Functional Keywords: phage lysozyme, sm-sad, atomic resolution, hydrolase
• Biological source: Enterobacteria phage P22
• Cellular location: Host cytoplasm : P09963
• Total number of polymer chains: 2
• Total formula weight: 34424.06

Authors

Mooers, B.H.,Matthews, B.W. (deposition date: 2005-08-11, release date: 2006-02-07, Last modification date: 2024-02-14)

Primary citation

Mooers, B.H.,Matthews, B.W.
Extension to 2268 atoms of direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme.
Acta Crystallogr.,Sect.D, 62:165-176, 2006

PubMed Abstract: The X-ray crystal structure of the previously unknown bacteriophage P22 lysozyme, the product of gene 19, has been determined ab initio by direct methods using the program SIR2002. The presence of several partially occupied iodine anions and samarium cations augmented the ability of direct methods to locate all 2268 non-H protein atoms in the asymmetric unit, making this one of the largest structures to date to be determined ab initio. The iodides were introduced from a quick soak, which the crystal survived sufficiently well to diffract to 1.04 angstroms resolution. The complete heavy-atom substructure contributed 6.6% of the total scattering power. The initial determination of the structure assumed that there were two iodide ions in the asymmetric unit, although it was later determined that these sites correspond to partially occupied samarium ions. Tests suggested that it is better to overestimate rather than underestimate the heavy-atom content. While experimental phases from all of the successful tests were of high quality, the best results came from a SAD experiment using the programs SHELXD and SHELXE. Nonetheless, ab initio structure determination by direct methods was found to be a viable alternative to traditional protein crystallographic methods provided that the X-ray data extend to atomic resolution and heavy atoms with sufficient scattering power are present in the crystal.

PubMed: 16421448
DOI: 10.1107/S0907444905037212

Experimental method

X-RAY DIFFRACTION (1.04 Å)