6533b85cfe1ef96bd12bd43c
RESEARCH PRODUCT
The hydration shell of myoglobin.
E. ClementiFritz G. ParakMarius SchmidtHermann HartmannGiorgina Corongiusubject
Electron densityMyoglobinProtein ConformationMonte Carlo methodBiophysicsWaterGeneral MedicineCrystal structureMolecular physicsCrystalCrystallographyReciprocal latticechemistry.chemical_compoundSolvation shellMyoglobinchemistryX-Ray DiffractionYield (chemistry)Monte Carlo MethodProtein Bindingdescription
The space in the unit cell of a metmyoglobin crystal not occupied by myoglobin atoms was filled with water using Monte Carlo calculations. Independent calculations with different amounts of water have been performed. Structure factors were calculated using the water coordinates thus obtained and the known coordinates of the myoglobin atoms. A comparison with experimental structure factors showed that both the low and the high resolution regime could be well reproduced with 814 Monte Carlo water molecules per unit cell with a B-value of 50 A2. The Monte Carlo water molecules yield a smaller standard R-value (0.166) than using a homogeneous electron density for the simulation of the crystal water (R = 0.212). A reciprocal space refinement of the water and the protein coordinates has been performed. Monte Carlo calculations can be used to obtain information for crystallographically invisible parts of the unit cell and yield better coordinates for the visible part in the refinement.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1992-11-01 | European biophysics journal : EBJ |