111L
STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
Experimental procedure
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.900, 60.900, 97.500 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | ? - 1.800 |
| R-factor | 0.155 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 2.000 |
| Refinement software | TNT |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 6.7 * | S. Dao-pin, (1990) Proteins Struct. Funct. Gen., 7, 198. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | 1.05 (M) | ||
| 2 | 1 | 1 | 1.26 (M) | ||
| 3 | 1 | 1 | 0.23 (M) | ||
| 4 | 1 | 1 | beta-mercaptoethanol | 1.4 (mM) |
