Salt is the only primary crystallization reagent (precipitant) utilized. Based on a design of 96 conditions, the screen evaluates a broad portfolio of crystallization salts of varying concentration and pH. The selection, concentration, and pH of the salts were determined by data mining the BMCD¹ and other crystallization databases, crystallization reports in the literature, and internal crystallization trials performed at Hampton Research. Based on this analysis, up to 35% of protein crystallizations involve salt as the primary crystallization reagent. SaltRx can be used as a primary crystallization screen when salt, ionic strength and pH are desired or suspected as appropriate crystallization variables. It is also useful as a secondary screen when salt only reagents/conditions from screens such as Index™, Crystal Screen™, and Grid Screen™ produce crystals and when further screening for additional salt conditions or optimization is desired. Since this screen does not contain volatile organics, it is compatible with microbatch, vapor diffusion, liquid and gel diffusion crystallization methods. SaltRx may also be used for dialysis crystallization in conjunction with Dialysis Buttons™.

The original SaltRx kit (HR2-108) contained 96 unique reagents, 10 ml each. This kit has been discontinued and converted into two 48 reagent based kits, SaltRx 1 and SaltRx 2, available separately, which when used together are identical to the original SaltRx.

SaltRx 1 contains 48 unique reagents, 10 ml each. SaltRx 1 contains reagents 1-48 of the original SaltRx 96 reagent kit.

Salt Rx 2 contains 48 unique reagents, 10 ml each. SaltRx 2 contains reagent 49-96 of the original SaltRx 96 reagent kit.

SaltRx HT contains the 96 SaltRx 1 and SaltRx 2 reagents in a single Deep Well block format.

Ready-to-use reagents are sterile filtered and formulated with ultra-pure Type 1 water, using the highest purity salts, polymers, organics and buffers. Individual reagents are available through the Hampton Research Custom Shop.

Measured pH range of kit is 4.1 to 9.0 at 25°C
Average measured pH of kit is 6.9 at 25°C
Median measured pH of kit is 7.3 at 25°C
Mode measured pH of kit is 7.4 at 25°C

应用
生物大分子的初级或次级、盐和pH基质结晶筛选
特征
盐与 pH 矩阵结晶筛选
样品 pH 值 4 至 9
22 种独特的盐与盐浓度和 pH 值的关系
与微批次、蒸汽扩散、液体和凝胶扩散方法兼容
管或深井块格式
预制，准备筛选
在汉普顿研究中心开发
屏幕中的所有盐和缓冲液均可作为 Optimize™ 试剂轻松获得，用于复制和优化晶体
可通过 Hampton Research Custom Shop 获得的个别试剂
描述
SaltRx 是由 Hampton Research 开发的，用于生物大分子的初级和次级、盐和 pH 值结晶筛选。盐是唯一使用的主要结晶试剂（沉淀剂）。该屏幕基于 96 种条件的设计，可评估各种不同浓度和 pH 值的结晶盐组合。盐的选择、浓度和 pH 值是通过对 BMCD1 和其他结晶数据库的数据挖掘、文献中的结晶报告以及在 Hampton Research 进行的内部结晶试验来确定的。根据这一分析，高达 35% 的蛋白质结晶涉及盐作为主要结晶试剂。当需要或怀疑盐分、离子强度和 pH 值是合适的结晶变量时，SaltRx 可用作主要结晶筛选。当 Index™、Crystal Screen™ 和 Grid Screen™ 等筛选中的仅含盐试剂/条件产生晶体时，以及需要进一步筛选其他盐条件或优化时，它也可用作二级筛选。由于该筛网不含挥发性有机物，因此与微批次、蒸汽扩散、液体和凝胶扩散结晶方法兼容。 SaltRx 还可与 Dialysis Buttons™ 结合用于透析结晶。

最初的 SaltRx 试剂盒 (HR2-108) 包含 96 种独特的试剂，每种试剂 10 毫升。该试剂盒已停产并转换为两个基于 48 试剂的试剂盒，SaltRx 1 和 SaltRx 2，单独提供，一起使用时与原始 SaltRx 相同。

SaltRx 1 包含 48 种独特的试剂，每种试剂 10 毫升。 SaltRx 1 包含原始 SaltRx 96 试剂盒的试剂 1-48。

Salt Rx 2 包含 48 种独特的试剂，每种试剂 10 毫升。 SaltRx 2 包含原始 SaltRx 96 试剂盒的试剂 49-96。

SaltRx HT 在单个 Deep Well 模块中包含 96 个 SaltRx 1 和 SaltRx 2 试剂。

即用型试剂经过无菌过滤和超纯 1 类水配制，使用最高纯度的盐、聚合物、有机物和缓冲液。个别试剂可通过 Hampton Research Custom Shop 购买。

试剂盒测得的 pH 值范围为 4.1 至 9.0 在 25°C
在 25°C 时，试剂盒的平均测量 pH 值为 6.9
试剂盒测得的 pH 中值在 25°C 时为 7.3
在 25°C 时，模式测量的试剂盒 pH 值为 7.4

CAT NO

SaltRx 1

SaltRx 2

SaltRx HT

 HR2-107 SaltRx 1 Documents HR2-107 SaltRx 1 SDS HR2-109 SaltRx 2 Documents HR2-109 SaltRx 2 SDS HR2-136 SaltRx HT Documents HR2-136 SaltRx HT SDS SaltRx Formulation & Scoring Data

1. Cloning, expression, purification and preliminary X-ray diffraction studies of a mycobacterial protein implicated in bacterial survival in macrophages. A. E. Shahine, P. Y. Chan, D. Littler, J. Vivian, R. Brammananth, P. K. Crellin, R. L. Coppel, J. Rossjohn and T. Beddoe. Acta Cryst. (2013). F69, 566-569.

2. Gilliland, G.L., Tung, M., Blakeslee, D.M. and Ladner, J. 1994. The Biological Macromolecule Crystallization Database, Version 3.0: New Features, Data, and the NASA Archive for Protein Crystal Growth Data. Acta Crystallogr. D50 408-413.

3. Crystallization and preliminary crystallographic analysis of molybdenum-cofactor biosynthesis protein C from Thermus thermophilus. S. P. Kanaujia, C. V. Ranjani, J. Jeyakanthan, S. Baba, L. Chen, Z.-J. Liu, B.-C. Wang, M. Nishida, A. Ebihara, A. Shinkai, S. Kuramitsu, Y. Shiro, K. Sekar and S. Yokoyama. Acta Cryst. (2007). F63, 27-29.

4. Crystal-contact engineering to obtain a crystal form of the Kelch domain of human Keap1 suitable for ligand-soaking experiments. Stefan Horer, Dirk Reinert, Katja Ostmann, Yvette Hoevels and Herbert Nar. Acta Cryst. (2013). F69, 592-596.