Open AccessGeneralized X‐ray and neutron crystallographic analysis: more accurate and complete structures for biological macromolecules
Author(s) -
Adams Paul D.,
Mustyakimov Marat,
Afonine Pavel V.,
Langan Paul
Publication year - 2009
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444909011548
Subject(s) - macromolecule , simulated annealing , crystallography , molecule , neutron , chemistry , materials science , protein structure , computer science , physics , algorithm , biochemistry , organic chemistry , quantum mechanics
X‐ray and neutron crystallographic techniques provide complementary information on the structure and function of biological macromolecules. X‐ray and neutron (XN) crystallographic data have been combined in a joint structure‐refinement procedure that has been developed using recent advances in modern computational methodologies, including cross‐validated maximum‐likelihood target functions with gradient‐based optimization and simulated annealing. The XN approach for complete (including hydrogen) macromolecular structure analysis provides more accurate and complete structures, as demonstrated for diisopropyl fluorophosphatase, photoactive yellow protein and human aldose reductase. Furthermore, this method has several practical advantages, including the easier determination of the orientation of water molecules, hydroxyl groups and some amino‐acid side chains.